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Enzymatic Modification of Starch: Amylases and Pullulanase

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dc.contributor.author Saeid, Abu
dc.contributor.author Akter, Farzana
dc.contributor.author Ali, Md. Aslam
dc.contributor.author Rahman, Md. Hafizur
dc.date.accessioned 2025-11-13T03:22:12Z
dc.date.available 2025-11-13T03:22:12Z
dc.date.issued 2024-06-20
dc.identifier.uri http://dspace.daffodilvarsity.edu.bd:8080/handle/123456789/15523
dc.description Book Chapter en_US
dc.description.abstract Starch-modifying enzymes are crucial biocatalysts with unique properties, versatile modes of action, and wide-ranging applications. These enzymes, often sourced from microorganisms, plants, or animals, operate under mild conditions, demonstrating high catalytic efficiency, substrate specificity, and eco-friendliness. In terms of mode of action, amylases (α-amylase and β-amylase) hydrolyze starch by cleaving α-1,4-glycosidic bonds or removing maltose units. Glucoamylase converts maltose and isomaltose into glucose. Starch phosphorylases introduce phosphate groups, yielding phosphorylated products, while debranching enzymes like pullulanase facilitate access to branched starch regions. Unlike non-food applications span numerous industries, modified starch is now employed in several food application such as bakery products, snacks, soups, sauces and gravies, batters and coatings, and meat products due to their numeral functional properties. However, starch-modifying enzymes, characterized by their properties, mode of action, and applications, are indispensable biocatalysts that continue to drive innovation across diverse sectors and sustainable industrial practices. This chapter focused on the major properties, mechanisms of action, and industrial applications of starch-modified enzymes. en_US
dc.language.iso en_US en_US
dc.subject Starch en_US
dc.subject Starch-modifying enzyme en_US
dc.subject Functional properties en_US
dc.subject Amylase en_US
dc.subject Glucoamylase en_US
dc.title Enzymatic Modification of Starch: Amylases and Pullulanase en_US
dc.type Book chapter en_US


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