Evidence map›Paper›PMID 33827572›Full record

ArticleMicrobial cell factories2021

Biochemical and synergistic properties of a novel alpha-amylase from Chinese nong-flavor Daqu.

Lanchai Chen, Zhuolin Yi, Yang Fang, Yanling Jin, Kaize He, Yao Xiao, Dong Zhao, Huibo Luo, Hui He, Qun Sun and 1 more

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 18 citations in OpenAlex.

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  7. Linking Microbial Functional Gene Abundance andFoods (Basel, Switzerland) · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Lanchai Chen *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, 610041, Sichuan, People's Republic of China.
Zhuolin Yi *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, 610041, Sichuan, People's Republic of China.
Yang FangCAS 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, 610041, Sichuan, People's Republic of China.
Yanling JinCAS 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, 610041, Sichuan, People's Republic of China.
Kaize HeCAS 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, 610041, Sichuan, People's Republic of China.
Yao XiaoAnalytical and Testing Center, Sichuan University of Science and Engineering, Zigong, 643000, China.
Dong ZhaoWuliangye Group, Yibin, 644007, China.
Huibo LuoLiquor Making Bio-Technology and Application of Key Laboratory of Sichuan Province, Bioengineering College, Sichuan University of Science and Engineering, Zigong, 643000, China.
Hui HeDepartment of Liquor Making Engineering, Moutai College, Renhuai, 564501, China.
Qun SunKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, No. 24 South Section 1, Yihuan Road, Chengdu, 610065, People's Republic of China. qunsun@scu.edu.cn.
Hai ZhaoCAS 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, 610041, Sichuan, People's Republic of China. zhaohai@cib.ac.cn.ORCID http://orcid.org/0000-0002-6116-6149
Chinese Academy of Sciences · CNSichuan University of Science and Engineering · CNHuaihua University · CNSichuan University · CN

Funding

Biological Resources Service Network Initiative of the Chinese Academy of Sciences ZSTHKey Deployment Project of the Chinese Academy of Sciences ZDRW-ZS-2017-2-1the China Agriculture Research System CARS-10-B22the National Key Research and Development Project 2019YFE0103800the National Natural Science for General Foundation of China 31770395
6 · The paper itself

Abstract

backgroundDaqu is the most important fermentation starter for Chinese liquor, with large number of microbes and enzymes being openly enriched in the Daqu system over thousands of years. However, only a few enzymes have been analyzed with crude protein for total liquefying power and saccharifying power of Daqu. Therefore, the complex enzymatic system present in Daqu has not been completely characterized. Moreover, their pivotal and complicated functions in Daqu are completely unknown.

resultsIn this study, a novel α-amylase NFAmy13B, from GH13_5 subfamily (according to the Carbohydrate-Active enZYmes Database, CAZy) was successfully heterologous expressed by Escherichia coli from Chinese Nong-flavor (NF) Daqu. It exhibited high stability ranging from pH 5.5 to 12.5, and higher specific activity, compared to other GH13_5 fungal α-amylases. Moreover, NFAmy13B did not show activity loss and retained 96% residual activity after pre-incubation at pH 11 for 21 h and pH 12 for 10 h, respectively. Additionally, 1.25 mM Ca

conclusionsThis study mined a novel GH13_5 fungal α-amylase (NFAmy13B) with outstanding alkali resistance from Nong-flavor (NF) Daqu. Furthermore, its synergistic effect with NFAmy13A (GH13_1) on hydrolyzing wheat starch was confirmed, and their possible contribution in NF Daqu was also speculated. Thus, we not only provide a candidate α-amylase for industry, but also a useful strategy for further studying the interactions in the complex enzyme system of Daqu.

Indexed as

Alcoholic Beveragesalpha-AmylasesFungiHydrolysisStarchalpha-AmylasesStarchAlkali‐resisting α-amylaseDaquGH13_5 subfamilySynergistic action

Identifiers

PMID33827572
PMCPMC8028695
OpenAlexW3150893870

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.