ArticleFoods (Basel, Switzerland)2022
Substrate Selectivity of a Novel Amylo-α-1,6-glucosidase from
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Discovery and structural analysis of glycoside hydrolase family 176 α-1,2 glucosidase from Arthrobacter humicola A8F5.The Journal of biological chemistry · 2026Article
- Structural Reconstruction and Enhanced Digestive Resistance in High-Amylose Maize Starch-Fatty Acid Complexes via Debranching and Heat-Moisture Treatment.Foods (Basel, Switzerland) · 2026Article
- Insights into the bacterial fraction of sediments from the South China Sea: physiological, chemotaxonomic, and genomic characterization of seven novel members of theFrontiers in microbiology · 2025Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Amylo-α-1,6-glucosidase (EC 3.2.1.33, AMY) exhibits hydrolytic activity towards α-1,6-glycosidic bonds of branched substrates. The debranching products of maltodextrin, waxy corn starch and cassava starch treated with AMY, pullulanase (EC 3.2.1.41, PUL) and isoamylase (EC 3.2.1.68, ISO), were investigated and their differences in substrate selectivity and debranching efficiency were compared. AMY had a preference for the branched structure with medium-length chains, and the optimal debranching length was DP 13-24. Its optimum debranching length was shorter than ISO (DP 25-36). In addition, the debranching rate of maltodextrin treated by AMY for 6 h was 80%, which was 20% higher than that of ISO. AMY could decompose most of the polymerized amylopectin in maltodextrin into short amylose and oligosaccharides, while it could only decompose the polymerized amylopectin in starch into branched glucan chains and long amylose. Furthermore, the successive use of AMY and β-amylase increased the hydrolysis rate of maltodextrin from 68% to 86%. Therefore, AMY with high substrate selectivity and a high catalytic capacity could be used synergistically with other enzyme preparations to improve substrate utilization and reduce reaction time. Importantly, the development of a novel AMY provides an effective choice to meet different production requirements.
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