ArticleBiotechnology for biofuels2021
Synergistic effects of multiple enzymes from industrial Aspergillus niger strain O1 on starch saccharification.
Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 24 citations in OpenAlex.
- Valorization of Stale Bread and Sunflower Spent Oil via Solid State Fermentation Using Food-Grade Filamentous Fungi.Biotech (Basel (Switzerland)) · 2026Article
- Development of an efficient heterologous protein expression platform in Aspergillus niger through genetic modification of a glucoamylase hyperproducing industrial strain.Microbial cell factories · 2025Article
- Article
- Manipulation of an α-glucosidase in the industrial glucoamylase-producingFrontiers in microbiology · 2022Article
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10 authors at 1 institution in 2 countries.
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Abstract
backgroundStarch is one of the most important renewable polysaccharides in nature for production of bio-ethanol. The starch saccharification step facilitates the depolymerization of starch to yield glucose for biofuels production. The filamentous fungus Aspergillus niger (A. niger) is the most used microbial cell factory for production of the commercial glucoamylase. However, the role of each component in glucoamylases cocktail of A. niger O1 for starch saccharification remains unclear except glucoamylase.
resultsIn this study, we identified the key enzymes contributing to the starch saccharification process are glucoamylase, α-amylase and acid α-amylase out of 29 glycoside hydrolases from the 6-day fermentation products of A. niger O1. Through the synergistic study of the multienzymes for the starch saccharification in vitro, we found that increasing the amount of α-amylase by 5-10 times enhanced the efficiency of starch saccharification by 14.2-23.2%. Overexpression of acid α-amylase in strain O1 in vivo increased the total glucoamylase activity of O1 cultures by 15.0%.
conclusionsOur study clarifies the synergistic effects among the components of glucoamylases cocktail, and provides an effective approach to optimize the profile of saccharifying enzymes of strain O1 for improving the total glucoamylase activity.
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