Comp Rev Food Sci Food Safe - 2022 - Dong - A Comprehensive Overview of Emerging Processing Techniques and Detection

Received: 3 January 2022 Revised: 3 May 2022 Accepted: 5 May 2022
DOI: 10.1111/1541-4337.12987
COMPREH ENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY
A comprehensive overview of emerging processing

techniques and detection methods for seafood allergens
Xin Dong Vijaya Raghavan
Department of Bioresource Engineering,

Faculty of Agricultural and Abstract
Environmental Sciences, McGill Seafood is rich in nutrients and plays a significant role in human health. How-
University, Sainte-Anne-de-Bellevue,
Quebec, Canada
ever, seafood allergy is a worldwide health issue by inducing adverse reactions
ranging from mild to life-threatening in seafood-allergic individuals. Seafood
Correspondence consists of fish and shellfish, with the major allergens such as parvalbumin and
Xin Dong, Department of Bioresource
Engineering, Faculty of Agricultural and tropomyosin, respectively. In the food industry, effective processing techniques
Environmental Sciences, McGill are applied to seafood allergens to lower the allergenicity of seafood products.
University, Sainte-Anne-de-Bellevue,
Also, sensitive and rapid allergen-detection methods are developed to identify
Quebec H9×3V9, Canada.
Email: [email protected] and assess allergenic ingredients at varying times. This review paper provides
an overview of recent advances in processing techniques (thermal, nonthermal,
A comprehensive overview on techniques
combined [hybrid] treatments) and main allergen-detection methods for seafood
Funding information products. The article starts with the seafood consumption and classification,
China Scholarship Council, Grant/Award proceeding with the prevalence and symptoms of seafood allergy, followed by
Number: 202008880002; Natural Sciences
and Engineering Research Council of
a description of biochemical characteristics of the major seafood allergens. As
Canada, Grant/Award Number: the topic is multidisciplinary in scope, it is intended to provide information for
RGPIN-2014-04190 further research essential for food security and safety.
KEYWORDS
allergen, ELISA, food safety, nonthermal processing, seafood
1 INTRODUCTION ous countries (Ruethers et al., 2018). In 2014, total seafood

production was estimated at 167 million tonnes worldwide;
Seafood is important to human health as it is a naturally per capita annual consumption of seafood products was
functional and highly nutritious food. Seafood is gener- more than two times in 2014 of over 20 kg compared with
ally considered as an invaluable protein resource. It was that in 1960 of at most 10 kg (FAO, 2016). Although seafood
reported that seafood proteins account for at least 20% of plays a significant role in the human diet, it is one of
animal protein intake in over 3.1 billion people (FAO, 2016). the key allergenic foods, which has the capacity to trigger
Seafood encompasses numerous essential micronutrients anaphylaxis among seafood-allergic individuals.
such as polyunsaturated fatty acids (PUFA), vitamins (A, Patients suffering from seafood allergies may fail to
B, and D), and trace minerals (calcium, iron, zinc, and identify the offending seafood species due to the diversity
selenium) (Dasanayaka et al., 2020). Furthermore, seafood of seafood products and their different common names
contains abundant omega-3 fatty acids, which can decrease (Davis et al., 2020). Besides, some irregular phenomenon
the risk for heart disease and ischemic stroke by regular in marketing including fraudulent substitution and mis-
intake of 1–2 times per week (Rimm et al., 2018). With great labeling have been noticed in many seafood products,
popularity among consumers, seafood products keep up especially in fish (Willette et al., 2017). Thus, it is impor-
with an increasing trend in international trade across vari- tant for patients to distinguish and identify their specific
3540 © 2022 Institute of Food Technologists.

R wileyonlinelibrary.com/journal/crf3 Compr Rev Food Sci Food Saf. 2022;21:3540–3557.
15414337, 2022, 4, Downloaded from https://ift.onlinelibrary.wiley.com/doi/10.1111/1541-4337.12987 by Mcgill University, Wiley Online Library on [27/03/2024]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
PROCESSING & DETECTION FOR SEAFOOD ALLERGEN 3541
FIGURE 1 Classification of common edible seafoods
allergenic seafood for better avoidance (Davis et al., 2020). 2 SEAFOOD ALLERGY PREVALENCE
As shown in Figure 1, edible seafood can be generally clas- AND SYMPTOMS
sified into fish (vertebrates) and shellfish (invertebrates).
Subsequently, edible fish species are mainly categorized as Seafood allergy is comprised of fish allergy and shellfish
bony fish and cartilaginous fish, which are in the phylum allergy, which belongs to two of the “big eight” allergenic
of Chordata. Within fish allergy, bony fish (cod, salmon, foods, fish and crustacean (Dong et al., 2021a). Fish allergy
and catfish) allergy has been reported more than carti- affects approximately 7% of pediatric populations world-
laginous fish (ray, shark, and ghost shark) allergy due to wide, and crustacean ranks as the third in order of the
the higher allergenicity of bony fish (Kalic et al., 2019). “big eight” allergenic foods only after peanut and tree nut
Notably, the patient allergic to one fish species may have by affecting over 2% of the population in the world
an almost 50% possibility to be cross-reactive to another (Buyuktiryaki et al., 2021; Laly & Sankar, 2020).
fish species (Kobayashi et al., 2016). Edible shellfish con- Moonesinghe et al. (2016) reported the global preva-
sists of crustacean and mollusk, belonging to the phyla lence of fish allergy and shellfish allergy ranging from
of Arthropoda and Mollusca (Ruethers et al., 2018). Crus- 0% to 7% and 0% to 10.3%, respectively. Studies suggest
tacean constitutes a diverse set of species such as prawns, that fish allergy prevalence is similar worldwide, whereas
shrimps, crabs, and lobsters, which are classified as arthro- shellfish allergy prevalence is significantly correlated
pods together with dust mites, spiders, and insects like to geography with higher prevalence in several regions,
cockroaches (Kamath et al., 2017). Mollusk also contains a such as Australia, Asia, the United States, and Europe
large group of species and can be broadly subdivided into (Moonesinghe et al., 2016). Moreover, shellfish is iden-
three classes (bivalve, cephalopod, and gastropod). Among tified as the major causative leading to anaphylaxis in
them, several main species are commonly consumed by Southeast Asia, Hongkong, and Taiwan, probably due
humans, comprising squid (calamari), abalone, mussels, to the high consumption of shellfish in the local diet of
oysters, scallops, clams, and cockles. Crustacean and mol- the population (Laly & Sankar, 2020; Moonesinghe et al.,
lusk clinically implicate cross-reactivity in many species 2016).
due to their panallergens (Ruethers et al., 2018). Fish allergy and shellfish allergy are both thought to be
In this review, we will explain the global prevalence, persistent, although their natural history is still unknown.
immunological mechanism, and symptoms of seafood Fish allergy generally develops early in life, whereas
allergy. Through careful examination of the main aller- shellfish allergy develops later, from adolescence onward
gens in seafood, current methods of seafood processing (Ebisawa et al., 2015). It has been concluded that both fish
techniques (thermal and nonthermal), applied to reduce allergy and shellfish allergy are usually induced through
seafood allergenicity, and seafood allergenicity detection three channels, including food intake, direct skin con-
methods will be comprehensively explored and discussed. tact, and breathing of the odors (Laly & Sankar, 2020). In
Furthermore, clinical diagnosis and medical treatments most cases, hyperallergic consumers suffer from seafood
of seafood allergy will also be summarized for the best allergy by ingesting specific allergic seafood; the aller-
management of seafood-allergic patients. genic ingredients may trigger allergic responses from
3542 PROCESSING & DETECTION FOR SEAFOOD ALLERGEN
TA B L E 1 Common clinical manifestations of seafood allergy

Organ involved Severity Typical symptoms
Skin Mild Mild rashes, hives (urticaria), swelling (angioedema),
palate itching, generalized pruritus
Gastrointestinal tract Mild Vomiting, nausea, abdominal cramping, diarrhea
Respiratory tract Mild Laryngospasm, wheezing, upper airway obstruction,
asthma (might severe)
Cardiovascular system Mild Hypotension
Ocular Mild Conjunctivitis
Neurological system Severe Loss of consciousness
Multi-organ (probably) Life-threatening Anaphylaxis
mild to life-threatening by entering the intestinal tract fish species (JF, 2003). Interestingly, among tilapia-allergic
and contacting with the mucosal immune system, which individuals, tropomyosin, a major shellfish allergen, was
is similar to other food allergies (Dong et al., 2021a; also characterized as a fish allergen (R. Liu et al., 2013).
Palomares, 2013). The clinical manifestations of seafood It has been reported that the tilapia allergen demonstrates
allergy may vary within an individual and between indi- high homology to human tropomyosin and potentially trig-
viduals (Khora, 2020) (Table 1). To date, the best way to gers inflammatory bowel diseases (Annette Kuehn et al.,
avoid suffering from food allergies is to avoid the intake of 2014).
the potential allergens for seafood-allergic patients (Dong As mentioned before, tropomyosin is the major aller-
et al., 2021a). gen in shellfish and responsible for ingestion-related
allergic reactions (Prester, 2016). Tropomyosin is a mus-
cle protein with a molecular weight of 34−38 kDa. It
3 SEAFOOD MAIN ALLERGENS belongs to the family of actin filament-binding proteins
with distinguished isoforms to express in muscle and
So far, there are 12 allergens in different fish species, which nonmuscle tissues (Khora, 2016). Table 2 summarizes var-
have been identified by the WHO/IUIS (Table 2). Parvalbu- ious tropomyosins identified in different shellfish species.
min and tropomyosin are the predominant allergens in fish Besides, tropomyosin is known as a pan-allergen with high
and shellfish, respectively (Fu et al., 2019). They are highly cross-reactivity in related species, such as crustaceans,
heat-stable and biochemical-stable allergens, which may insects, and various classes of mollusks (Wild & Lehrer,
in part explain the persistence of seafood allergy (Ebisawa 2005). The molecular homology of tropomyosin existing in
et al., 2015). The parvalbumin family comprises two iso- shellfish species is very high, especially within the same
form lineages, parvalbumin α and parvalbumin β, in which species. It was reported that the homology between various
parvalbumin β is recognized as the major fin fish allergen. crustacean species is approximate 98%, and the homology
Parvalbumins are calcium-binding muscle proteins with between molluscan is up to 68−100% (Lee et al., 2012). It is
low molecular weight ranging from 9 to 14 kDa (X. Zhang estimated that 75% of patients allergic to one shellfish have
et al., 2021). They are highly thermostable and abundantly risks to be allergic to another shellfish. Thus, all shellfish-
exist in fast twitching white muscle entailed for calcium allergic patients are suggested to avoid the intake of all
signaling. The Ca2+ coordinating amino acid residues are shellfish products due to the highly cross-reactive aller-
known for their contribution to the conformational IgE gens present in shellfish species. In addition, other main
epitopes. The first identified fish parvalbumin is a Baltic seafood allergens are also identified, such as beta-enolase,
cod allergen (Gad c 1) in the early 1970s, followed by other collagen, and gelatine in fish, and arginine kinase, myosin
parvalbumins widely existing in commonly consumed fish light chain, and sarcoplasmic calcium-binding protein in
species, such as cod, carp, and herring (Elsayed & Aas, shellfish (Table 2) (Ayuso et al., 2008; Hamada et al., 2001).
1971; A Kuehn et al., 2013; Lim et al., 2008). The homology Notably, up to 6% of seafood-allergic patients have aller-
of amino acids among different fish species is very high, gic reactions to both shellfish and fish allergens, and hence
reaching 60–90%, such as in cod, carp, hake, chub, and it is generally unnecessary for the avoidance of both fish
Atlantic salmon (Bugajska-Schretter et al., 1998). Due to and shellfish due to no cross-reactivity between parvalbu-
the cross-reactivity, people allergic to one fish species have min and tropomyosin (Khan et al., 2011; Lopata & Lehrer,
approximately a 50% chance to react adversely to another 2009).
TA B L E 2 Main allergens identified in fish and shellfish (data from www.allergen.org)

Molecular
Category Biomedical name wright/kDa Allergen Main species
Fish Beta parvalbumin 11–12 Lep w 1 Megrim, whiff, turbot fish
Pan h 1 Striped catfish
Seb m 1 Ocean perch, redfish,
Xip g 1 snapper
Clu h 1 Swordfish
Cyp c 1 Atlantic herring
Gad c 1 Common carp
Sal s 1 Baltic cod
Thu a 1 Atlantic salmon
Yellowfin tuna
Beta enolase 47–50 Pan h 2 Striped catfish
Cyp c 2 Common carp
Gad m 2 Atlantic cod
Sal s 2 Atlantic salmon
Thu a 2 Yellowfin tuna
Aldolase A 40 Pan h 3 Striped catfish
Gad m 3 Atlantic cod
Thu a 3 Yellowfin tuna
Tropomyosin 35–36 Lep s 1 Silverfish
Pro c 1 Red swamp crayfish
Collagen alpha 130–140 Lat c 6 Barramundi
Creatine kinase 43 Pan h 7 Striped catfish
Triosephosphate isomerase 25–28 Arc s 8 Crayfish
Pro c 8 Red swamp crayfish
Pyruvate kinase PKM-like 65 Pan h 9 Striped catfish
Beta-prime-component of 18 Onc k 5 Chum salmon
vitellogenin
l-lactate dehydrogenase 34 Pan h 10 Striped catfish
Glucose 6-phosphate isomerase 60 Pan h 11 Striped catfish
Glyceraldehyde-3-phosphate 36 Pan h 13 Striped catfish
dehydrogenase
Shellfish Tropomyosin 34–38 Pen i 1 Shrimp
Cra c 1 North Sea shrimp
Cra g 1 Pacific oyster
Exo m 1 White legged freshwater
Mel l 1 shrimp King prawn
Scy p 1 Mud crab
Arginine kinase 40–45 Lit v 2 White shrimp
Pen m 2 Black tiger shrimp
Scy p 2 Mud crab
Myosin light chain 17.5–23 Cra c 5 North Sea shrimp
Hom a 3 American lobster
Lit v 3 White shrimp
Pen m 3 Black tiger shrimp
Scy p 3 Mud crab
Sarcoplasmic calcium-binding 20–25 Cra c 4 North Sea shrimp
protein Cra a 4 Pacific oyster
Lit v 4 White shrimp
Scy p 4 Mud crab
4 EFFECTS OF PROCESSING
TECHNIQUES ON SEAFOOD
ALLERGENICITY
In recent years, different processing (thermal and nonther-

mal) techniques are applied to seafood products to reduce
their allergenicity with the least loss in nutritional value
and sensory quality. After processing, biochemical charac-
teristics of allergenic proteins may be altered and chemical
reactions in the seafood matrix components occur.
Importantly, the type and conditions of the processing
techniques applied can variably affect seafood allergenicity
(Jiménez-Saiz et al., 2015). Table 3 summarizes recent
advances in the impacts of processing techniques (ther- F I G U R E 2 Effect of thermal treatment on epitopes in
mal/ nonthermal/combined (hybrid) treatments) on allergenic protein
seafood allergenicity. For various fish and shellfish prod-
ucts, processing might cause an increase, decrease, or no
effect in their allergenicity. unfolding in allergens leading to the exposure of their
conformational epitopes.
Oppositely, high-intensity microwave treatment
4.1 Thermal treatment (75−125◦ C for 5−15 min) could significantly reduce the
allergenicity of shrimp (Litopenaeus vannamei) by 75%
In fish products, wet-heat treatment (100◦ C for 45 min) determined by a sandwich ELISA test (Dong et al.,
decreased the IgG binding in parvalbumins within 2021b). This is because higher temperatures might reduce
37 kinds of southern hemisphere fish species from allergenicity because irreversible aggregation with cova-
Australia by a quantitative detection, Western blot (Liang lent and hydrophobic interactions may occur after an
et al., 2021). Moreover, heating (20−140◦ C) muscle extracts extremely high-intensity thermal processing (Arámburo-
from Pacific mackerel parvalbumin caused a reduction Galvez et al., 2018; Peram et al., 2013). Whereas in another
in the IgE reactivity of the parvalbumin determined by study, crab (Scylla paramamosain) tropomyosin treated by
ELISA using human sera, with a complete decline of IgE boiling (100◦ C for 15 min) and steaming (100◦ C for 20 min)
reactivity observed at 140◦ C heating (Kubota et al., 2016). demonstrated no obvious distinction in immunoreactivity
In addition, heat processing (95◦ C for 15 min) was applied measured by SDS–PAGE (M. Liu et al., 2018). Similarly,
to parvalbumin in a diversity of bony and cartilaginous no changes were observed in the antigenicity of purified
fish from the Asia-Pacific region; the results showed that tropomyosin (Pen j 1) from raw kuruma prawns (Marsupe-
such thermal treatment caused a decline in the antibody naeus japonicus) after heat treatment (20−80◦ C) analyzed
reactivity to multimeric parvalbumins for most bony fish, by SDS–PAGE and Western blotting (Usui et al., 2013).
and a complete reduction of reactivity for cartilaginous As discussed earlier, thermal treatment is commonly
fish measured by molecular analysis and Western blot used to process seafood products to both affect seafood
(Saptarshi et al., 2014). However, the allergenicity of puri- allergenicity by conformational changes in allergens and
fied cod parvalbumin treated by heat (25–105◦ C) exhibited influence the interactions in seafood ingredients. The rea-
no alterations by utilizing an indirect noncompetitive sons can be that allergenic protein molecules are unfolded
ELISA test with allergic-patient sera (Somkuti et al., 2012). causing a loss in their secondary and tertiary struc-
In shellfish products, an enhanced intensity of tures, which further leads to covalent and noncovalent
tropomyosin band in shrimp (Penaeus monodon) was interactions between intra and/or intermolecules. Confor-
observed during SDS–PAGE analysis of extracts by heat mational epitopes in allergenic protein can be expressed
treatments, including steaming (3 min), baking (200◦ C or destroyed thereby affecting allergenicity, whereas the
for 4 min), frying (> 200◦ C for 1 min), microwave roasting linear epitopes remain unaltered (Figure 2) (Rahaman
(at power level 3 for 2 min), grilling (> 250◦ C for 7 min), et al., 2016). Despite the wide application of thermal pro-
and boiling (5 min) (Lasekan & Nayak, 2016). Besides, cessing, nonthermal methods are being considered for
fresh raw shrimp after a thermal treatment (boiling at reducing seafood allergenicity due to their better perfor-
100◦ C for 15 min) showed higher IgE-binding activity and mance in preserving the original characteristics of seafood,
immunoreactivity as per the results from SDS-PAGE. The such as maintaining the organoleptic properties, color, and
increase in allergenicity is probably due to the molecular nutrient contents (Shriver & Yang, 2011).
TA B L E 3 Effect of various processing techniques on seafood allergenicity
Seafood
Processing technique category Sample Treatment Detection method Result References
Thermal Wet-heat Fish 37 southern hemisphere 100◦ C for 45 min Western blot Decreased the IgG binding in (Liang et al., 2021)
processing fish species parvalbumins
Heat Muscle extracts from 20−140◦ C ELISA using human Reduced the IgE reactivity of the (Kubota et al.,
Pacific mackerel sera parvalbumin 2016)
parvalbumin
Heat Parvalbumin in diverse 95◦ C for 15 min Molecular analysis Reduced antibody reactivity in bony (Saptarshi et al.,
bony and and Western blot fish; a complete reduction in 2014)
cartilaginous fish cartilaginous fish
Heat purified cod 25-105◦ C Indirect No alterations (Somkuti et al.,
parvalbumin non-competitive 2012)
ELISA
PROCESSING & DETECTION FOR SEAFOOD ALLERGEN
Heat Shellfish Raw kuruma prawns 20−80◦ C SDS–PAGE and No changes (Usui et al., 2013)
(Marsupenaeus Western blotting
japonicus)
Boil Fresh raw shrimp 100◦ C for 15 min SDS–PAGE Increased IgE-binding activity and (Arámburo-
immunoreactivity Galvez et al.,
2018; Peram
et al., 2013)
Steam Shrimp (Penaeus 3 min SDS–PAGE An enhanced intensity of tropomyosin (Lasekan &
monodon) band Nayak, 2016)
Bake Shrimp (Penaeus 200◦ C for 4 min SDS–PAGE an enhanced intensity of tropomyosin (Lasekan &
Fry Shrimp (Penaeus >200◦ C for 1 min SDS–PAGE an enhanced intensity of tropomyosin (Lasekan &
Microwave roast Shrimp (Penaeus at power level 3 for SDS–PAGE an enhanced intensity of tropomyosin (Lasekan &
monodon) 2 min band Nayak, 2016)
Grill Shrimp (Penaeus >250◦ C for 7 min SDS–PAGE an enhanced intensity of tropomyosin (Lasekan &
Boil Shrimp (Penaeus 5 min SDS–PAGE an enhanced intensity of tropomyosin (Lasekan &
Boil Crab (Scylla 100 ◦ C for 15 min SDS–PAGE no obvious distinction in (M. Liu et al.,
paramamosain) immunoreactivity 2018)
Steam Crab (Scylla 100 ◦ C for 20 min SDS–PAGE no obvious distinction in (M. Liu et al.,
paramamosain) immunoreactivity 2018)
Microwave shrimp (Litopenaeus 2.45 GHz, 1000 W, Sandwich ELISA and A maximum reduction of 75% (Dong et al.,
vannamei) 75−125◦ C for SDS–PAGE 2021b)
5−15 min
3545
(Continues)
TA B L E 3 (Continued)
3546
Seafood
Nonthermal High hydrostatic Fish Cultured large yellow 300-600 MPa for SDS–PAGE Reduced the allergenicity (H. Zhang et al.,
processing pressure croakers 10 min 2020)
(Larimichthys crocea)
Drying Atlantic cod Indirect competitive Increased the IgE binding activity (Sletten et al.,
ELISA 2010)
Marinade Moroccan fish species Marinade with ELISA Reduced Immunoreactivity (Mejrhit et al.,
in Fez region olive oil, lemon 2018).
(sardine, common juice, salt, pepper
pandora, and shrimp) and garlic for a day
at 4◦ C
Fermentation Moroccan fish species Ferment crushed ELISA Immunoreactivity all reduced; (Mejrhit et al.,
in Fez region shrimp mixed with maximum reduction in IgG binding 2018).
(sardine, common salt for several were marked in fermented sardine of
pandora, and shrimp) weeks 64.5%, and in fermented shrimp of
69.2%
High pressure Shellfish Tropomyosin in crab 0.08 MPa for 15 min Western blotting, Reduced the immunoreactivity of (M. Liu et al.,
(Scylla SDS–PAGE and tropomyosin 2018)
paramamosain) inhibition ELISA
Extraction buffers Pacific oyster with PH value of SDS–PAGE more IgE-reactive bands on (Nugraha et al.,
(Crassostrea gigas) 3.0-10.3 immunoblotting in high pH buffers; 2021)
less IgE-reactivities in low pH buffers
Enzymatic hydrolysis Tropomyosin in shrimp Pepsin and pancreatin Western blot Tropomyosin remains stable and (Toomer et al.,
extracts immunoreactive 2015)
Ultrasound shrimp (Litopenaeus 5-20 min at room Sandwich ELISA and A maximum reduction of 76% (Dong et al., 2020)
vannamei) temperature SDS–PAGE
Electron beam Shrimp (Solenocera Doses of 0, 1, 3, 5, 7, Indirect ELISA Decrease the IgG binding capacity and (Guan et al., 2018)
irradiation melantho) 9 kGy, rate of analysis and immunoreactivity of tropomyosin
1 kGy/s Western blot
Combined Thermal-glycation Fish Purified Alaska pollock Glycation with Indirect competitive Enhanced IgE/IgG binding capacities in (M. Zhang et al.,
processing Parvalbumin glucose, fructose, ELISA the parvalbumins glycated with 2021)
ribose, lactose, and glucose and fructose; while a loss of
galactose at 60◦ C IgE/IgG binding capacities in the
for 1 h parvalbumins glycated with ribose,
lactose, and galactose
Thermal-glycation Recombinant silver Glucose at 60◦ C for 72 Dot blot Reduced IgE binding (Y.-J. Zhao et al.,
carp parvalbumin h 2017)
(Continues)
TA B L E 3 (Continued)
Seafood
Thermal-glycation Fish protein Glycation with ribose Histamine release Reduced the allergenicity (Yang et al., 2015)
hydrolysates at 121◦ C for
30–90 min
Hot-smoked Antigenic proteins in 70−80◦ C for 16 min Indirect Slightly decreased immunoreactivity (Zhu & Hsieh,
fish samples (carp, non-competitive 2021)
Atlantic herring, and enzyme-linked

Sockeye salmon) immunosorbent
assay and Dot blot
High-temperature Shellfish Edible portions in fresh 0.08 MPa, 115◦ C, Western blotting Reduced the immunoreactivity (M. Liu et al.,
pressure raw shrimp 15 min 2019)
High-temperature Shrimp (Litopenaeus 0.08 MPa at 110–121◦ C SDS–PAGE and A significant decline in the (M. Liu, Huan,
pressure combined vannamei) for 6 min; glycation Western blotting IgG/IgE-binding activity et al., 2021a)
with glycation with galactose
High-pressure Shrimp (Penaeus 0.14 MPa at 121◦ C for SDS–PAGE lower IgE binding capacity (Lasekan &
steaming monodon) 20 min Nayak, 2016).
Pressure combined Shrimp (Metapenaeus Pressure for 5–20 min; SDS–PAGE and significant reduction of IgE activity and (S J et al., 2021)
with soaking dobsoni soaking in salt, immunoblotting a absent tropomyosin band in shrimp
baking soda, papain extracts; significant increase in IgE
and acetic acid) activity and retained tropomyosin
band in peeled shrimp
High-temperature Crab (Scylla 0.08 MPa, 115◦ C, Basophil activation Decreased the allergenicity (M. Liu, Han,
pressure paramamosain) 15 min test et al., 2021b)
Thermal-glycation Tropomyosin in Scallop Glycation with xylose Dot blotting, western Reduced IgE binding activity and (Bai et al., 2021)
(Chlamys nobilis) at 30−100◦ C blotting, Inhibition immunoreactivity
ELISA
3547
4.2 Nonthermal treatment centration, time duration, and so on. Other than low-
ering seafood allergenicity, nonthermal processing can
For fish products, high hydrostatic pressure (300–600 MPa significantly inactivate microorganisms without heating to
for 10 min) treatment could effectively reduce the aller- preserve sensory quality and nutritive value in seafood,
genicity of cultured large yellow croakers (Larimichthys and also further assuring seafood safety and extending
crocea) by altering the stability of the secondary and ter- the shelf-life (Olatunde et al., 2021). Therefore, nonther-
tiary structure of parvalbumin (H. Zhang et al., 2020). mal processing is regarded as a well-balanced technique
Conversely, drying increased the IgE binding activity in between safety and minimal processing, between accept-
Atlantic cod tested by an indirect competitive ELISA able quality and economic constraints, and between novel
(Sletten et al., 2010). In another study, three commonly processing resources and traditional processing techniques
consumed Moroccan fish species in the Fez region (sar- (H. Q. Zhang et al., 2011).
dine, common pandora, and shrimp) were processed
by canning, marinade, and fermentation; ELISA results
showed that all the processing methods resulted in a loss 4.3 Combined (hybrid) treatment
of the immunoreactivity of human IgE to fish species,
with a better performance after treatments by marinade In fish products, purified Alaska pollock parvalbumin
and fermentation. The maximum reduction in IgG binding was glycated with glucose, fructose, ribose, lactose, and
was marked in fermented sardine at 64.5% and fermented galactose at 60◦ C for 1 h; the enhanced IgE/IgG bind-
shrimp at 69.2% (Mejrhit et al., 2018). ing capacities were observed in the parvalbumins glycated
For shellfish products, the allergenicity of shrimp with glucose and fructose, while there was a loss of
(Litopenaeus vannamei) treated by ultrasound (5-20 min at IgE/IgG binding capacities in the parvalbumins glycated
room temperature) showed a significant decline of 76% in with ribose, lactose, and galactose analyzed by the indirect
tropomyosin measured by a sandwich ELISA (Dong et al., competitive ELISA. The converse results were probably
2020). Electron beam irradiation (doses of 0, 1, 3, 5, 7, because different reducing sugars exhibited various glyca-
9 kGy, rate of 1 kGy/s) could also decrease the IgG bind- tion effects on modifying protein conformations, causing
ing capacity and immunoreactivity of tropomyosin from the differences in specific recognition of antigen and anti-
Solenocera melantho due to the changes in the secondary body (M. Zhang et al., 2021). Similarly, thermal-glycation
structure of shrimp tropomyosin (Guan et al., 2018). Simi- treatment (glucose at 60◦ C for 72 h) also led to a reduc-
larly, the immunoreactivity of tropomyosin in crab (Scylla tion of IgE binding in recombinant silver carp parvalbumin
paramamosain) was obviously reduced after high-pressure detected by Dot blot (Y.-J. Zhao et al., 2017). Also, the
treatment at 0.08 MPa for 15 min detected by Western blot- allergenicity in fish protein hydrolysates analyzed through
ting, inhibition ELISA, and SDS–PAGE (M. Liu et al., a response surface methodology reduced after the treat-
2018). ment of glycation with ribose at 121◦ C for 30–90 min (Yang
Alternatively, eight different extraction buffers (with et al., 2015). Interestingly, antigenic proteins in fish sam-
a PH value of 3.0-10.3) were applied to protein in ples (carp, Atlantic herring, and Sockeye salmon) were
Pacific oyster (Crassostrea gigas) using serum from five retained even after single processing conditions of salt-
shellfish-allergic patients; the results revealed more IgE- ing, smoking, and heating (boiling 0−8 min) treatment
reactive bands on immunoblotting in high pH buffers, tested by both indirect ELISA and dot blot. However, a
and fewer IgE-reactivities in low pH buffers (Nugraha slight decrease in immunoreactivity was observed when
et al., 2021). In addition, tropomyosin in shrimp extracts hot smoked treatment was applied at 70−80◦ C for an addi-
remained stable and immunoreactive after in-vitro gas- tional 8 min, revealing that repeated heating might degrade
tric digestion (pepsin and pancreatin) determined by or aggregate the antigens (Zhu & Hsieh, 2021).
Western blot, whereas epitope-binding capacity predom- In shellfish products, high-temperature pressure
inately decreased after pancreatin digestion possibly due (0.08 MPa, 115◦ C, 15 min) could decrease the allergenic-
to the denatured and destroyed secondary and/or tertiary ity in crab (Scylla paramamosain) tropomyosin as per
conformations (Toomer et al., 2015). basophil activation test due to the alteration in the protein
It has been assessed that nonthermal processing can structure such as denaturation (M. Liu, Han, et al., 2021a).
effectively change the allergenicity or immunoreactiv- Tropomyosin from autoclaved shrimp (Penaeus monodon)
ity of seafood proteins because irreversible alterations in had a lower IgE binding after high pressure steaming
secondary, tertiary, and quaternary structures of aller- (0.14 MPa at 121◦ C for 20 min) analyzed by SDS–PAGE
genic proteins occurred by influencing the covalent bonds. (Lasekan & Nayak, 2016). Also, a high-temperature
Such alterations are mostly affected by treatment con- pressure treatment (0.08 MPa, 115◦ C, 15 min) in auto-
ditions, such as treatment power, frequency/rate, con- claving can reduce the immunoreactivity of the edible
portions in fresh raw shrimp observed by using Western (ELISA), polymerase chain reaction (PCR), lateral flow
blotting measurement. Such results were induced by the device (LFD)/dipstick, lateral flow immunoassay (LFIA),
macrostructural and microstructural alterations in shrimp liquid chromatography-mass spectrometry (LC-MS), and
samples, including interactions between the multicom- biosensors. Nevertheless, ELISA, LFD, and PCR are the
ponents and allergens in the food matrix (M. Liu et al., only methods commercially available for detecting and
2019). quantifying allergens in fish (Ruethers et al., 2020).
Shrimp (Litopenaeus vannamei) processed by Maillard
reaction (glycation with galactose) with high temperature–
pressure (0.08 MPa at 110–121◦ C for 6 min) showed a sig- 5.1 Enzyme-linked immune sorbent
nificant decline in the IgG/IgE-binding activity due to the assay (ELISA)
modified macrostructure of lysine, arginine, and cysteine
residues in antigen epitopes (M. Liu, Huan, et al., 2021b). A ELISA is the most common method to quantify allergenic
thermal-glycation method, Maillard-reacted tropomyosin protein in food products. It is based on monoclonal or poly-
(TM epitopes with lysine and arginine), could signifi- clonal antibody recognition of one or more allergens in
cantly decrease the IgE binding activity and further result food products, with a detection limit of ∼0.1−5 mg/kg and
in lower immunoreactivity in Scallop (Chlamys nobilis) as parts per million (ppm) (Monaci & Visconti, 2010). As
by destroying and masking saccharide residues on the shown in Figure 3A, four types of ELISA assays are usu-
tropomyosin surface (Bai et al., 2021). In another study, ally used for allergen detection, including direct, indirect,
shrimp (Metapenaeus dobsoni) was pretreated into both sandwich, and competitive ELISA (Hidayat & Wulandari,
shrimp extracts and peeled shrimps, and then treated by 2021). In experimental protocol, ELISA analysis consists of
pressure (5-20 min) combined with soaking treatments a series of incubation and wash steps after protein extrac-
(in salt, baking soda, papain, and acetic acid). The results tion. It finally acquires sample concentration relying on
of shrimp extracts indicated that there was a significant a standard curve generated by a diluted allergenic pro-
reduction of IgE activity and an absence of tropomyosin tein standard (Karsonova et al., 2020). ELISA analysis has
band in the immunoblot using pooled sera of the shrimp- been widely used in the routine detection of food allergens,
allergic patient, whereas a converse result was observed because it is mature, easy, and provides high sensitivity and
in peeled shrimp with significantly increasing IgE activ- specificity.
ity and retained tropomyosin band due to the retention In a study focusing on epitope analysis, an indi-
of allergenicity in peeled shrimps. Such different results rect ELISA was used to characterize the IgE-binding
might be explained by increasing rigidity in shrimp tis- and IgG4 -binding to a major fish allergen Lat c 1.01
sue induced by the gestalt-binding interactions between (Sharp et al., 2021). Moreover, ELISA was also applied
tropomyosin and actin (Holmes & Lehman, 2008). to investigate the IgE sensitization/cross-linking capac-
Physical food processing techniques are powerful in ity of fish collagen among 101 fish-allergic individuals,
eliminating seafood allergens, but most combined (hybrid) which is a new finding for collagen in diagnostic tests and
treatments (combining thermal and nonthermal process- it further helped to improve patient safety (Kalic et al.,
ing) show a better performance than single treatments (Fu 2020). In addition, the capacity of various ELISA tests
et al., 2019). Therefore, based on current study findings in might help demonstrate their usefulness through their
eliminating seafood allergens, there is a greater likelihood varied results. Ruethers et al. (2020) reported that three
of making seafood accessible for hyperallergic consumers. commercial ELISA kits demonstrated a limited capacity
and distinguished detection rates in the detection of both
raw and heated extracts from bony fish (26−61%), canned
5 DETECTION METHODS FOR bony fish (65−86%), and cartilaginous fish (0%). Besides,
SEAFOOD ALLERGENS Dasanayaka et al. (2021) developed a new sandwich ELISA
method, which was based on goat IgG (capturing anti-
As discussed earlier, the allergenicity of the same pro- body) and rabbit IgG (detecting antibody) targeting soluble
tein might exhibit differences in different matrices, which antigenic fish proteins (detection targets) to detect unde-
is probably affected by a number of factors such as clared fish residues in foods and thereby reduce the
matrix, antibody, and detection approaches (Griesmeier incidents of fish allergies. Recently, J. Zhao et al. (2022) also
et al., 2010). To assess seafood allergen, novel detec- developed a poly- and monoclonal antibody-based (PcAb
tion measurements with high sensitivity and efficiency and mAb) sandwich ELISA method to detect crustacean
are necessary (Fu et al., 2019). To date, detection and tropomyosin in foods, and this novel method showed
quantification methods applied to food allergen sources better matrix-tolerance and detectability in processed
generally include enzyme-linked immune sorbent assay foods.
FIGURE 3 (A) Four types of ELISA assays used for allergen detection (B) Schematic diagram of lateral flow immunoassay
As studies described, ELISA analysis, a protein-based 5.2 Polymerase chain reaction (PCR)
assay, shows an overall sufficient sensitivity in the simul-
taneous quantification of seafood proteins. However, dif- PCR technology is a highly specific and automatic DNA-
ferent processing methods, antibody composition, exper- based methodology used to monitor allergenic ingredients
imental operations, reagents, and standards may cause during seafood processing. DNA methodologies are indi-
large quantitative differences in allergenic proteins, and rect in detecting seafood allergens as they detect the DNA
also false positive or false negative results (Asensio et al., sequences from the allergenic food components rather
2008; Parker et al., 2015). Moreover, another inconvenience than detecting the allergenic protein itself (Broeders et al.,
of the immunoassays is that protein solubility might be 2012). With high sensitivity, even small amounts of DNA
altered by processing techniques, which can affect the copies can be detected using specific PCR. Besides, DNA
subsequent detection with protein-based approaches (Mat- has a more stable performance than proteins, especially in
tison et al., 2016). Instead, other detection methods, such as thermal treatments. (M. Sun et al., 2009).
DNA-based assays, are necessary for seafood analytic tests For the detection of potentially allergenic proteins in
since DNA molecules can maintain their integrity better seafood, various PCR assays have been described. A
than proteins (A Kuehn et al., 2017). study verified that both commercial real-time PCR (DNA-
based) and ELISA kits (immunochemical approach) can tides. The peptide mixtures generated will be within a
recognize shrimp allergens in kimchi, saeu-jeot, and saeu- specific range for LC-MS analysis. Subsequently, LC-MS
aekjeot, however, with variable sensitivities. The variations separates these peptides based on differences in their rel-
are caused by the detection limits and different reactivities ative affinity to the stationary phase (column) and the
to shrimp allergens, including tropomyosin and sarcoplas- mobile phase (solvent). Electrospray ionization is con-
mic calcium-binding protein (Jeong & Kim, 2020). In ducted by eluting and ionizing, and it is consequently
addition, quantitative real-time PCR with a specific primer through LC-MS (Croote & Quake, 2016).
pair, Tropo-F and Tropo-R, could be successful for the Lv et al. (2020) established the liquid chromatography-
identification and quantitative analysis of the presence tandem mass spectrometry (LC–MS/MS) method with
of tropomyosin in shrimp (Phan et al., 2020). Besides, high sensitivity and selectivity for simultaneously quanti-
Eischeid (2019) also used a real-time PCR method to detect fying biomarkers and validated it in a cell model during
cod and pollock in complex food matrices (cooking oil, allergy-related research. Based on liquid chromatography-
clam chowder, and hushpuppy mix) and achieved low tandem mass spectrometry and multiple reaction mon-
detection limits at 1−10 mg/kg. Similarly, Fernandes et al. itoring mass spectrometry (LC-MRM-MS/MS), a new
(2018) proposed and compared two real-time PCR systems approach was developed with simple, sensitive, and accu-
based on a TaqMan probe and the EvaGreen dye. They rate advantages. This method utilized a thermal purifica-
found that both systems are precise, but the probe sys- tion procedure followed by a completely optimized tryptic
tem demonstrated higher sensitivity and dynamic range digestion. In this study, parvalbumin beta in flounder (Par-
(0.0001−50%) than the EvaGreen (0.05−50%). Other than alichthys olivaceus) has been successfully determined at
using PCR assay alone, a multiplex PCR assay combined a low level to the extent of 0.10 μg/g with satisfactory
with capillary electrophoresis was developed to detect accuracy and precision (L. Sun et al., 2019). Similarly,
tropomyosin genes in oyster, mussel, abalone, and clam, Stella et al. (2020) established a method coupling liq-
and the 18S rRNA gene in eukaryotes. The results showed uid chromatography with high-resolution tandem mass
that this assay is very useful and efficient in detecting spectrometry (LC-HRMS/MS) to select marker peptides
tropomyosin allergens from mollusk species in seafood in allergens and simultaneously detect crustaceans. The
(Suh et al., 2020). method has been validated in fish contaminated at 10 μg/g
Until now, plenty of useful PCR assays have been for crustaceans (Stella et al., 2020). J. Wang et al. (2021)
established in related research. Advantages of DNA- also developed an assay based on high-performance liquid
based assays compared with protein-based methodologies chromatography-tandem mass spectrometry (LC–HRMS)
include that the target DNA can be efficiently extracted to detect crustacean TM qualitatively and quantitatively.
from uncooked or cooked products almost without being They found that this approach demonstrated high accu-
affected by thermal processing. This is because DNA racy and reproducibility (recovery range of 91−109%, stan-
exposed to the cooking temperatures can remain frag- dard deviations < 15%, limit of quantification of 1.6 mg/kg)
mented but detectable in seafood products (Linacero et al., in various food matrices (chicken sausages, beef balls, and
2020). Although some food components may interfere with egg–milk biscuits).
the PCR assay to reduce the amplification efficiency, PCR Furthermore, LC-MS has been developed for both online
inhibitors can be removed during DNA extraction and and offline quantification of seafood allergens based on
purification procedures with the help of suitable DNA target peptides, which is especially suitable for the deter-
clean-up steps (López-Calleja et al., 2007). In recent years, mination of seafood allergens during seafood processing
PCR technology is becoming popular to be used in detect- due to its indifference to conformational protein epitopes.
ing food allergens, but with some limitations, such as However, further studies are needed on the application of
unsuitable for the identification of targeting allergenic pro- LC-MS for seafood allergen detection, since the high cost of
teins with unidentified genes in food matrices (van Hengel, professional mass spectrometry equipment and advanced
2007). Thus, more efforts in the development of detection operating techniques may lead to some limitations for wide
methods are needed with further refinement. application in the food industry (Bereszczak & Brancia,
2009).
5.3 Liquid chromatography-mass
spectrometry (LC-MS)
5.4 Lateral flow device (LFD) and
Liquid chromatography-mass spectrometry is regarded as lateral flow immunoassay (LFIA)
a sensitive multiplexed quantification method for food
allergens. In experiments, extracted proteins are reduced, The LFD/dipstick is a qualitative or semiquantitative tool
alkylated, and then enzymatically hydrolyzed into pep- to be implemented in food allergen analysis. It is relatively
easy to operate, portable, and inexpensive. The method The SPR biosensor is applied to the high-throughput
involves the application of test antigen/analyte and anti- analysis of food allergens. SPR biosensor aims to measure
body with a membrane, such as nitrocellulose, nylon, or the refractive index changes based on the surface plasmon,
polyvinylidene difluoride (Sharma et al., 2017). LFIA serves which is induced by the biomolecules interacting with the
as a semiquantitative method using visual signals to indi- surface of SPR biosensors. It is relatively simple, inexpen-
cate allergens detected. The principle of LFIA operation sive, and easy to use compared to other biosensors (Šípová
is based on allergen interaction with antibodies, demon- & Homola, 2013). SPR serves as a highly sensitive optical
strating the test results through antibody-coated colored sensing approach and can realize the real-time monitoring
particles (Figure 3B) (Xu et al., 2021). of small changes in the effective refractive index of a metal–
Koizumi et al. (2014) developed and validated a sensitive dielectric interface (Michel et al., 2017). Zhou et al. (2020)
and visual lateral flow assay for detecting shrimp allergenic proposed an SPR biosensor method with gold patterned
protein. The detection limit for shrimp protein extract was biochips to detect and quantify shellfish tropomyosin; they
25 μg/L, equivalent to 1 μg/g protein in a food sample; found that this developed methodology to be suitable for
the test results could be obtained within 20 min with- the determination of tropomyosin from various shellfish
out sophisticated procedures or expensive equipment. The species in 3 min, which was a very accurate and rapid
concordance was up to 97% between LFD and validated technology (Zhou et al., 2020).
ELISA for commercially processed foods (Koizumi et al., Except for the SPR biosensor, Chinnappan et al. (2020)
2014). Zheng et al. (2012) developed a quantitative LFIA developed an aptamer biosensor for the detection of
based on a superparamagnetic nanoparticle (SPMNP) shrimp tropomyosin. This aptamer-based sensor success-
probe for the fish major allergen, parvalbumin. Compara- fully detected tropomyosin in 30 min with sensitive, selec-
tive test results indicated that the relative consistency was tive, and specific advantages (Chinnappan et al., 2020). In
93.1% between the LFIA and Western blot assay in 29 food addition, a gold nanoparticle-based label-free colorimetric
extract samples. Besides, the detection time of the LFIA assay was proposed as a visual colorimetric detection tech-
approach was within 20 min whereas the Western blot nology to detect the shrimp tropomyosin. The aptasensor
assay commonly takes about 5 h (Zheng et al., 2012). After- is highly reliable, selective, and sensitive with the observed
ward, Y. Wang et al. (2019) designed quantum-dot-based detection limitation of 70 nmol/L in shrimp (Pavase et al.,
LFIA to detect crustacean tropomyosin with a limitation 2021). However, it was reported that the aptamer stability
of 0.5 μg/ml visually and 0.05 μg/ml by instrument. The and function might be altered due to the instability and
LFIA has been verified as a specific and reproducible assay relative nonspecific binding of aptamers (Stoltenburg et al.,
with consistent and comparable test results to the validated 2007).
ELISA kit (Y. Wang et al., 2019).
LFD and LFIA usually demonstrate advantages, includ-
ing quick response (within several minutes), high sen- 5.6 Comparison between
sitivity, visible test results, and ease of usage, although allergen-detection methods
some of them are mono-color and unstable (Y. Wang
et al., 2019). Therefore, LFD/LFIA, as a novel-developed Table 4 summarizes the advantages and disadvantages of
detection technology, is potentially anticipated to boost current seafood allergen-detection methods. According to
the applications for the on-site detection of tropomyosin the present studies, there is no doubt that immunoassays,
(Galan-Malo et al., 2019). including Indirect ELISA and Western blot, are the main
detection methods in investigating the processing effect on
fish allergens. The mechanisms are clarified in that the
5.5 Biosensors binding between antibodies and processed allergenic pro-
teins lead to a modified capacity to elicit allergic reactions
Biosensors are considered as an alternative technology to (Verhoeckx et al., 2015). Nonetheless, immunoassay might
analyze and track food allergens. It is rapid, sensitive, be inaccurate, since it can present wrong results due to
selective, and available for site analysis, such as surface cross-reaction of the antibody with nontarget allergenic
plasmon resonance (SPR) biosensor, surface-enhanced proteins and not be efficient enough in allergen-detection
Raman spectroscopy (SERS), amperometric biosensors, procedure. On the contrary, LFIA is more efficient and reli-
voltammetric biosensors, quartz crystal microbalance able and can be operated for on-site detection (Xu et al.,
(QCM) biosensors and molecularly imprinted polymers- 2021). Compared with protein-based methods, LC-MS and
based (MIP) biosensors Nevertheless, biosensor tech- DNA-based methods have gradually gained more attention
niques generally require expensive instruments and skilled due to their inherent independence from biomolecular
operators (Zhou et al., 2019). interactions. However, they basically require unportable
TA B L E 4 Summarization of common allergen-detection methods for seafood products

Method Advantages Disadvantages
ELISA ∙ High sensitivity and specificity ∙ Results are easily affected by various factors
∙ Easy operation ∙ False positive or false negative results might be
∙ The most common method and has a wide obtained
application ∙ Protein can be altered after processing
PCR ∙ Stable to maintain the integrity even after ∙ Unsuitable to identify target allergenic proteins
thermal processing with unidentified genes
∙ High sensitivity and efficiency ∙ More expensive than protein-based methods
∙ Less prone to contamination
LC-MS ∙ High sensitivity and accuracy ∙ Expensive and unportable professional equipment
∙ Improved reproducibility ∙ Requiring specialized and complex operating
∙ Dynamic range techniques
LFD/LFIA ∙ On-site detection method ∙ Mono-color

∙ High sensitivity and efficient ∙ Instability
∙ Visible test results
∙ Ease of usage
∙ Cheap
Biosensors ∙ Rapid ∙ Instability

∙ Sensitive and selective ∙ Low affinity
∙ Available for site analysis
∙ Ease of usage
and expensive equipment with specialized and complex the single treatments, combined (hybrid) treatments have
operations (Holzhauser & Röder, 2015). In recent years, better performance with higher efficiency in eliminat-
biosensors are widely applied in allergen detection, such ing seafood allergens. It is to be noted that the inves-
as multiplex detection, on-site quantitative detection, and tigations by main allergen-detection methods include
even unknown allergens detection. Although it is a sen- ELISA, PCR, LFD/LFIA, LC-MS, and biosensors; all of
sitive, rapid, and easy measurement method, the device them show their various advantages and disadvantages.
format may lead to some restrictions in allergen-detection The development of reliable, rapid, and on-site allergen-
applications (Xu et al., 2021). detection methods showing high accuracy and sensitivity
Therefore, reliable, high-throughput, and real-time are future research trends for seafood products. How-
detection methods with high accuracy and sensitivity are ever, the avoidance of allergenic seafood intake is still
crucially required in detecting allergenic ingredients in the only standard way to clinically protect seafood-allergic
seafood products. This is meaningful to monitor cross- patients. Therefore, in-depth research is necessary to
contamination during seafood processing to further reduce decrease the risk of seafood allergy and create an accessi-
the risks of allergen cross-contamination and also to avoid ble and safe environment for worldwide customers in the
allergen intake accidentally to some extent. future.
AC K N OW L E D G M E N T S
6 CONCLUSION The authores appreciate the financial support from the
Natural Sciences and Engineering Research Council of
Seafood allergy is a global health problem. Both fish Canada (NSERC) [RGPIN-2014-04190] and the China
and shellfish allergies may affect human life quality Scholarship Council [202008880002].
with mild or severe symptoms. Seafood processing tech-
niques, including thermal, nonthermal, and combined AU T H O R CO N T R I B U T I O N S
(hybrid) treatments, are powerful in reducing allergenic- Xin Dong: Conceptualization; data curation; formal
ity by modifying the allergen conformations. Compared analysis; investigation; methodology; software; writing—
to thermal treatments, nonthermal treatments usually original draft; writing—review & editing. Vijaya G.S.
show better results in retaining the nutritional value Raghavan: Funding acquisition; project administration;
and sensory quality of seafood products. Compared to resources; supervision; writing—review & editing
CONFLICTS OF INTEREST Davis, C. M., Gupta, R. S., Aktas, O. N., Diaz, V., Kamath, S. D., &
The authors declare no conflict of interest in this paper. Lopata, A. L. (2020). Clinical management of seafood allergy. The
Journal of Allergy and Clinical Immunology: In Practice, 8(1), 37–
44.
ORCID
Dong, X., Wang, J., & Raghavan, V. (2020). Effects of high-intensity
Xin Dong https://orcid.org/0000-0002-9052-3563
ultrasound processing on the physiochemical and allergenic prop-
erties of shrimp. Innovative Food Science & Emerging Technologies,
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Received: 3 January 2022 Revised: 3 May 2022 Accepted: 5 May 2022

COMPREH ENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY

A comprehensive overview of emerging processing

Xin Dong Vijaya Raghavan

Department of Bioresource Engineering,

1 INTRODUCTION ous countries (Ruethers et al., 2018). In 2014, total seafood

3540 © 2022 Institute of Food Technologists.

FIGURE 1 Classification of common edible seafoods

TA B L E 1 Common clinical manifestations of seafood allergy

TA B L E 2 Main allergens identified in fish and shellfish (data from www.allergen.org)

In recent years, different processing (thermal and nonther-

Atlantic herring, and enzyme-linked

TA B L E 4 Summarization of common allergen-detection methods for seafood products

LFD/LFIA ∙ On-site detection method ∙ Mono-color

Biosensors ∙ Rapid ∙ Instability

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