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Insight into broad substrate specificity and synergistic contribution of a fungal α-glucosidase in Chinese Nong-flavor daqu.

التفاصيل البيبلوغرافية
العنوان: Insight into broad substrate specificity and synergistic contribution of a fungal α-glucosidase in Chinese Nong-flavor daqu.
المؤلفون: Yi Z; CAS Key Laboratory of Environmental and Applied Microbiology, Environmental Microbiology Key Laboratory of Sichuan Province, Chengdu Institute of Biology, Chinese Academy of Sciences, No. 9 Section 4, Renmin Nan Road, Chengdu, Sichuan, 610041, P.R. China., Chen L; School of Food and Bioengineering, Xihua University, Chengdu, Sichuan, 610039, China., Jin Y; CAS Key Laboratory of Environmental and Applied Microbiology, Environmental Microbiology Key Laboratory of Sichuan Province, Chengdu Institute of Biology, Chinese Academy of Sciences, No. 9 Section 4, Renmin Nan Road, Chengdu, Sichuan, 610041, P.R. China., Shen Y; Sichuan Langjiu Co., Ltd, Gulin, 646523, China., Liu N; Sichuan Food and Fermentation Industry Research & Design Institute, Chengdu, 611130, China., Fang Y; CAS Key Laboratory of Environmental and Applied Microbiology, Environmental Microbiology Key Laboratory of Sichuan Province, Chengdu Institute of Biology, Chinese Academy of Sciences, No. 9 Section 4, Renmin Nan Road, Chengdu, Sichuan, 610041, P.R. China., Xiao Y; Analytical and Testing Center, Sichuan University of Science and Engineering, Zigong, 643000, China., Wang X; Sichuan Langjiu Co., Ltd, Gulin, 646523, China., Peng K; Sichuan Food and Fermentation Industry Research & Design Institute, Chengdu, 611130, China., He K; CAS Key Laboratory of Environmental and Applied Microbiology, Environmental Microbiology Key Laboratory of Sichuan Province, Chengdu Institute of Biology, Chinese Academy of Sciences, No. 9 Section 4, Renmin Nan Road, Chengdu, Sichuan, 610041, P.R. China., Zhao H; CAS Key Laboratory of Environmental and Applied Microbiology, Environmental Microbiology Key Laboratory of Sichuan Province, Chengdu Institute of Biology, Chinese Academy of Sciences, No. 9 Section 4, Renmin Nan Road, Chengdu, Sichuan, 610041, P.R. China. zhaohai@cib.ac.cn.
المصدر: Microbial cell factories [Microb Cell Fact] 2023 Jun 15; Vol. 22 (1), pp. 114. Date of Electronic Publication: 2023 Jun 15.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: BioMed Central Country of Publication: England NLM ID: 101139812 Publication Model: Electronic Cited Medium: Internet ISSN: 1475-2859 (Electronic) Linking ISSN: 14752859 NLM ISO Abbreviation: Microb Cell Fact Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London : BioMed Central, [2002-
مواضيع طبية MeSH: alpha-Glucosidases*/genetics , Fermentation* , Alcoholic Beverages*, alpha-Amylases ; Glucose ; Starch ; Substrate Specificity
مستخلص: Background: Chinese Nong-favor daqu, the presentative liquor starter of Baijiu, has been enriched with huge amounts of enzymes in degrading various biological macromolecules by openly man-made process for thousand years. According to previous metatranscriptomics analysis, plenty of α-glucosidases were identified to be active in NF daqu and played the key role in degrading starch under solid-state fermentation. However, none of α-glucosidases was characterized from NF daqu, and their actual functions in NF daqu were still unknown.
Results: An α-glucosidase (NFAg31A, GH31-1 subfamily), the second highest expressed α-glucosidases in starch degradation of NF daqu, was directly obtained by heterologous expression in Escherichia coli BL21 (DE3). NFAg31A exhibited the highest sequence identities of 65.8% with α-glucosidase II from Chaetomium thermophilum, indicating its origin of fungal species, and it showed some similar features with homologous α-glucosidase IIs, i.e., optimal activity at pH ~ 7.0 and litter higher temperature of 45 ℃, well stability at 41.3 ℃ and a broad pH range of pH 6.0 to pH 10.0, and preference on hydrolyzing Glc-α1,3-Glc. Besides this preference, NFAg31A showed comparable activities on Glc-α1,2-Glc and Glc-α1,4-Glc, and low activity on Glc-α1,6-Glc, indicating its broad specificities on α-glycosidic substrates. Additionally, its activity was not stimulated by any of those detected metal ions and chemicals, and could be largely inhibited by glucose under solid-state fermentation. Most importantly, it exhibited competent and synergistic effects with two characterized α-amylases of NF daqu on hydrolyzing starch, i.e., all of them could efficiently degrade starch and malto-saccharides, two α-amylases showed advantage in degrading starch and long-chain malto-saccharides, and NFAg31A played the competent role with α-amylases in degrading short-chain malto-saccharides and the irreplaceable contribution in hydrolyzing maltose into glucose, thus alleviating the product inhibitions of α-amylases.
Conclusions: This study provides not only a suitable α-glucosidase in strengthening the quality of daqu, but also an efficient way to reveal roles of the complicated enzyme system in traditional solid-state fermentation. This study would further stimulate more enzyme mining from NF daqu, and promote their actual applications in solid-state fermentation of NF liquor brewing, as well as in other solid-state fermentation of starchy industry in the future.
(© 2023. The Author(s).)
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معلومات مُعتمدة: 2020XBZG_XBQNXZ_A_001 CAS "Light of West China" Program; 2023YFS0445 Sichuan Science and Technology Program; 2022YFN0043 Sichuan Science and Technology Program; CARS-10-GW24 the earmarked fund for CARS-10-Sweetpotato
فهرسة مساهمة: Keywords: Glycoside hydrolase family 31 (GH31); Heterologous expression; Liquor starter; Metatranscriptomics; α-Glucosidase (AG)
المشرفين على المادة: EC 3.2.1.1 (alpha-Amylases)
EC 3.2.1.20 (alpha-Glucosidases)
IY9XDZ35W2 (Glucose)
9005-25-8 (Starch)
تواريخ الأحداث: Date Created: 20230615 Date Completed: 20230620 Latest Revision: 20230620
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC10268404
DOI: 10.1186/s12934-023-02124-z
PMID: 37322438
قاعدة البيانات: MEDLINE
الوصف
تدمد:1475-2859
DOI:10.1186/s12934-023-02124-z