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    Introduction To Enymes

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    Meshal Noor
    Microbial enzymes are biological catalysts that speed up biochemical reactions. They can be extracted from cells and used commercially. Enzymes play roles in producing sweeteners, modifying antibiotics, and in cleaning and analytical products. Enzymes are potent and specific catalysts that convert substrates to products without being consumed. They are usually proteins that contain active sites which bind substrates. Cofactors such as vitamins and minerals are sometimes required for enzymatic activity.

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    Introduction To Enymes

    Uploaded by

    Meshal Noor
    43 views34 pages
    Microbial enzymes are biological catalysts that speed up biochemical reactions. They can be extracted from cells and used commercially. Enzymes play roles in producing sweeteners, modifying antibiotics, and in cleaning and analytical products. Enzymes are potent and specific catalysts that convert substrates to products without being consumed. They are usually proteins that contain active sites which bind substrates. Cofactors such as vitamins and minerals are sometimes required for enzymatic activity.

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    Microbial enzymes are biological catalysts that speed up biochemical reactions. They can be extracted from cells and used commercially. Enzymes play roles in producing sweeteners, modifying antibiotics, and in cleaning and analytical products. Enzymes are potent and specific catalysts that convert substrates to products without being consumed. They are usually proteins that contain active sites which bind substrates. Cofactors such as vitamins and minerals are sometimes required for enzymatic activity.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    43 views34 pages

    Introduction To Enymes

    Uploaded by

    Meshal Noor
    Microbial enzymes are biological catalysts that speed up biochemical reactions. They can be extracted from cells and used commercially. Enzymes play roles in producing sweeteners, modifying antibiotics, and in cleaning and analytical products. Enzymes are potent and specific catalysts that convert substrates to products without being consumed. They are usually proteins that contain active sites which bind substrates. Cofactors such as vitamins and minerals are sometimes required for enzymatic activity.

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    of 34

    Microbial Enzyme Technology

    By; Ms. Jawairia kiran


    Introduction to enzymes
    The nature and classification of enzymes
    • Enzymes are biological catalysts (also known as biocatalysts)

    • speed up biochemical reactions in living organisms

    • can also be extracted from cells and then used to catalyse a wide
    range of commercially important processes

    For example
    • Production of sweetening agents
    • Modification of antibiotics
    • Used in washing powders and various cleaning products
    • Play a key role in analytical devices and assays that have clinical,
    forensic and environmental applications.
    The word ‘enzyme’ was first used by the
    German physiologist Wilhelm Kühne in 1878
    • He was describing the
    ability of yeast to
    produce alcohol from
    sugars, and it is derived

    • From the Greek words :


    en (meaning ‘within’)
    zume (meaning ‘yeast’).
    • In the late nineteenth century and early twentieth
    century, significant advances were made in the
    extraction, characterization and commercial
    exploitation of many enzymes

    • 1920s that enzymes were crystallized, revealing that


    catalytic activity is associated with protein molecules.

    • For the next 60 years or so it was believed that all


    enzymes were proteins

    • In 1980s it was found that some ribonucleic acid (RNA)


    molecules are also able to exert catalytic effects called
    ribozymes, play an important role in gene expression.
    • In the same decade, biochemists developed
    the technology to generate antibodies that
    possess catalytic properties.

    • These so-called ‘abzymes’ have significant


    potential both as novel industrial catalysts and
    in therapeutics.
    • As catalysts, enzymes are required in very low
    concentrations

    • They speed up reactions without themselves


    being consumed during the reaction

    • Enzymes are describe as being capable of


    catalysing the conversion of substrate molecules
    into product molecules as follows:
    Substrate ⇌ Enzyme Product
    Enzymes are potent catalysts
    • The enormous catalytic activity of enzymes
    can be expressed by a constant, kcat referred as
    the turnover rate, turnover frequency or
    turnover number.

    • This constant represents the number of


    substrate molecules that can be converted to
    product by a single enzyme molecule per unit
    time (usually per minute or per second).
    Examples of turnover rate values are:
    For example

    Single molecule of carbonic anhydrase can


    catalyse the conversion of over half a million
    molecules of its substrates, carbon dioxide
    (CO2) and water (H2O), into the product,
    bicarbonate (HCO3−), every second—a truly
    remarkable achievement.
    Enzymes are specific catalysts
    • They generally catalyse the conversion of only
    one type (or at most a range of similar types)
    of substrate molecule into product molecules.
    • Some enzymes demonstrate group specificity.

    • For example, alkaline phosphatase can remove


    a phosphate group from a variety of
    substrates.
    • Other enzymes demonstrate much higher specificity,
    which is described as absolute specificity.

    • For example, glucose oxidase shows almost total


    specificity for its substrate, β-D-glucose, and virtually
    no activity with any other monosaccharides.

    • This specificity is of paramount importance in many


    analytical assays and devices (biosensors) that measure
    a specific substrate (e.g. glucose) in a complex mixture
    (e.g. a blood or urine sample).
    Enzyme names and classification
    • the enzyme committee (EC) of the International
    Union of Biochemistry and Molecular Biology
    (IUBMB) recommended the classification of
    enzymes into six groups.

    • The IUBMB committee also defines subclasses


    and sub-subclasses.

    • Each enzyme is assigned an EC (Enzyme


    Commission) number.
    For example
    The EC number of catalase is EC 1.11.1.6.
    The first digit indicates that the enzyme belongs to
    oxidoreductase (class1).
     Subsequent digits represent subclasses and sub-
    subclasses.
    • The enzyme rennet used in cheese
    manufacture and also known as chymosin, has
    the number of EC 5.3.1.5.
    The six major EC groups are as follows:
    1. Oxidoreductases :
    Catalyze a variety of oxidation-reduction reactions
    Common names include:
    dehydrogenase, oxidase, reductase and catalase.

    2. Transferases:
    Catalyze transfers of groups (acetyl, methyl, phosphate,
    etc.).
    Common names include acetyltransferase, methylase,
    protein kinase, and polymerase.
     The first three subclasses play major roles in the regulation
    of cellular processes.
    3. Hydrolases:
    Catalyze hydrolysis reactions where a molecule
    is split into two or more smaller molecules by
    the addition of water.
    Some examples are:
    i. Proteases: Proteases split protein molecules.

    • They are further classified by their optimum


    pH as acid, alkaline or neutral.

    • They may also be classified on the basis of


    their active centers into the following:
    a. Serine proteases:
    These have a residue in their active center and are
    specifically inhibited by diisopropyl
    phosphofluoridate and other organophosphorus
    derivates.

    b. Thiol proteases:
    • The activity of these depends on the presence of
    an intact-SH group in their active center.

    • They are specifically inhibited by thiol reagents


    such as heavy metal ions and their derivatives, as
    well as alkylating and oxidizing agents.
    c. Metal proteases: These depend on the
    presence of more of less tightly bound divalent
    cations for their activity.

    d. Acid proteases: Acid proteases contain one or


    more side chain carboxyl groups in their active
    center.
    ii. Nucleases split nucleic acids (DNA and
    RNA).

    • Based on the substrate type, they are divided


    into RNase and DNase.
    – RNase catalyzes the hydrolysis of RNA
    – DNase acts on DNA.
    • They may also be divided into Exonuclease
    and Endonuclease.
    – The exonuclease progressively splits off single
    nucleotides from one end of DNA or RNA.
    – The endonuclease splits DNA or RNA at internal
    sites.
    iii. Phosphatase catalyzes dephosphorylation
    (removal of phosphate groups).
    4. Lyases
    Catalyze the cleavage of C-C, C-O, C-S and C-N
    bonds by means other than hydrolysis or
    oxidation.
    Common names include decarboxylase and
    aldolase.
    5. Isomerases catalyze atomic rearrangements
    within a molecule.
    Examples include
    • rotamase, protein disulfide isomerase (PDI), epimerase
    and racemase.

    6. Ligases catalyze the reaction which joins two


    molecules.
    Examples include peptide
    • synthase, aminoacyl-tRNA synthetase, DNA ligase and
    RNA ligase.
    Enzyme structure and substrate
    binding
    • Amino acid-based enzymes are globular proteins

    • Range in size from less than 100 to more than 2000 amino
    acid residues.

    • These amino acids can be arranged as one or more


    polypeptide chains

    • that are folded and bent to form a specific three-


    dimensional structure, incorporating a small area known as
    the active site where the substrate actually binds
    • The active site may
    well involve only a
    small number (less
    than 10) of the
    constituent amino
    acids
    It is the shape and charge properties of the
    active site that enable it to bind to a single
    type of substrate molecule, so that the
    enzyme is able to demonstrate considerable
    specificity in its catalytic activity.
    • German chemist Emil Fischer in 1894, first
    proposed “Enzyme specificity results from the
    complementary nature of the substrate and its
    active site”

    Became known as Fischer's ‘lock and key


    hypothesis’
    • Through techniques such as X-ray
    crystallography, it became clear that enzymes
    are not rigid structures, but are in fact quite
    flexible in shape.

    • In 1958 Daniel Koshland extended Fischer's


    ideas and presented the ‘induced-fit model’ of
    substrate and enzyme binding
    • The enzyme molecule changes its shape
    slightly to accommodate the binding of the
    substrate
    • Large number of enzymes consist solely of protein, many
    also contain a non-protein component, known as a cofactor
    that is necessary for the enzyme's catalytic activity.

    • A cofactor may be another organic molecule called a


    coenzyme

    • or it may be an inorganic molecule, typically a metal ion


    such as iron, manganese, cobalt, copper or zinc.

    • A coenzyme that binds tightly and permanently to the


    protein is generally referred to as the prosthetic group of
    the enzyme.
    • When an enzyme requires a cofactor for its
    activity, the inactive protein component is
    generally referred to as an apoenzyme

    • the apoenzyme plus the cofactor (i.e. the


    active enzyme) is called a holoenzyme
    • The need for minerals and vitamins in the human diet is
    partly attributable to their roles within metabolism as
    cofactors and coenzymes.
    • Suggested books:
    1. Ray, R. C., 2005. Microbial Biotechnology in
    Agriculture and Aquaculture. NBN
    International.
    2. Kreuzer, H. and Massey, A., 2005. Biology and
    Biotechnology Science, Applications, and
    Issues American Society for Microbiology.
    Thank you

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