Exploring Amylolytic Enzymes from GH Families in Maltooligosaccharide Biosynthesis: Classification, Catalysis, and Industrial Potential

Amylolytic enzymes, including α-amylase, β-amylase, and glucoamylase, are crucial in starch degradation and maltooligosaccharide (MOS) biosynthesis. Glycoside hydrolases (GHs), notably from families GH13, GH14, GH15, GH57, GH119, and GH126, offer high substrate specificity and catalytic efficiency under mild conditions. Their ability to produce MOS with prebiotic and functional properties underpins their growing relevance in food, pharmaceutical, and biofuel industries. This review highlights the classification, catalytic mechanisms, sources, and production techniques of these enzymes. It also discusses critical factors affecting enzyme activity—pH, temperature, substrate concentration, and metal ion activators—and explores their structural and biochemical characteristics for industrial applications. Finally, challenges such as enzyme stability and cost-efficiency are outlined alongside future prospects involving synthetic biology and process optimization for sustainable MOS production.

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Publication Details

Journal
Zenodo (CERN European Organization for Nuclear Research)
Published
2025-06-30
DOI
https://doi.org/10.5281/zenodo.17212122
Primary Topic
Geochemistry and Geologic Mapping
Type
article
Field-Weighted Citation Impact
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article

Exploring Amylolytic Enzymes from GH Families in Maltooligosaccharide Biosynthesis: Classification, Catalysis, and Industrial Potential

Zenodo (CERN European Organization for Nuclear Research)
Geochemistry and Geologic Mapping
article

Exploring Amylolytic Enzymes from GH Families in Maltooligosaccharide Biosynthesis: Classification, Catalysis, and Industrial Potential

article en

Abstract

Amylolytic enzymes, including α-amylase, β-amylase, and glucoamylase, are crucial in starch degradation and maltooligosaccharide (MOS) biosynthesis. Glycoside hydrolases (GHs), notably from families GH13, GH14, GH15, GH57, GH119, and GH126, offer high substrate specificity and catalytic efficiency under mild conditions. Their ability to produce MOS with prebiotic and functional properties underpins their growing relevance in food, pharmaceutical, and biofuel industries. This review highlights the classification, catalytic mechanisms, sources, and production techniques of these enzymes. It also discusses critical factors affecting enzyme activity—pH, temperature, substrate concentration, and metal ion activators—and explores their structural and biochemical characteristics for industrial applications. Finally, challenges such as enzyme stability and cost-efficiency are outlined alongside future prospects involving synthetic biology and process optimization for sustainable MOS production.

Zenodo (CERN European Organization for Nuclear Research)
Sepuluh Nopember Institute of Technology (ID)
Industry, innovation and infrastructure
Openalex Percentile: Top 26%
Geochemistry and Geologic Mapping
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