Department of Biology, Faculty of Science and Data Analytics, Sepuluh Nopember Institute of Technology, Surabaya 60111, Indonesia.
International Journal of Science and Research Archive, 2025, 15(03), 1728-1736
Article DOI: 10.30574/ijsra.2025.15.3.1924
Received on 15 May 2025; revised on 23 June 2025; accepted on 25 June 2025
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.
Amylolytic enzyme; Glycoside hydrolases; Maltooligosaccharide; Biosynthesis
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Afifah Nurul Ilmi and Enny Zulaika. Exploring Amylolytic Enzymes from GH Families in Maltooligosaccharide Biosynthesis: Classification, Catalysis, and Industrial Potential. International Journal of Science and Research Archive, 2025, 15(03), 1728-1736. Article DOI: https://doi.org/10.30574/ijsra.2025.15.3.1924.
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