Production of marine bacterial metalloprotease A69 and evaluation of its potential in preparing soybean peptides with angiotensin-converting enzyme-inhibitory activity.


Journal

Journal of the science of food and agriculture
ISSN: 1097-0010
Titre abrégé: J Sci Food Agric
Pays: England
ID NLM: 0376334

Informations de publication

Date de publication:
Nov 2023
Historique:
revised: 07 06 2023
received: 19 03 2023
accepted: 20 06 2023
medline: 23 10 2023
pubmed: 20 6 2023
entrez: 20 6 2023
Statut: ppublish

Résumé

Marine bacteria secrete a variety of proteases, which are a good source to explore proteases with application value. However, only a few marine bacterial proteases with a potential in bioactive peptides preparation have been reported. The metalloprotease A69 from the marine bacterium Anoxybacillus caldiproteolyticus 1A02591 was successfully expressed in the food safe bacterium Bacillus subtilis as a secreted enzyme. A technique to efficiently produce protease A69 in a 15-L bioreactor was established, with a production of 8988 U mL The marine bacterial metalloprotease A69 has a promising potential for preparing SPs with good nutritional and potential antihypertensive effects, laying a good foundation for its industrial production and application. © 2023 Society of Chemical Industry.

Sections du résumé

BACKGROUND BACKGROUND
Marine bacteria secrete a variety of proteases, which are a good source to explore proteases with application value. However, only a few marine bacterial proteases with a potential in bioactive peptides preparation have been reported.
RESULTS RESULTS
The metalloprotease A69 from the marine bacterium Anoxybacillus caldiproteolyticus 1A02591 was successfully expressed in the food safe bacterium Bacillus subtilis as a secreted enzyme. A technique to efficiently produce protease A69 in a 15-L bioreactor was established, with a production of 8988 U mL
CONCLUSION CONCLUSIONS
The marine bacterial metalloprotease A69 has a promising potential for preparing SPs with good nutritional and potential antihypertensive effects, laying a good foundation for its industrial production and application. © 2023 Society of Chemical Industry.

Identifiants

pubmed: 37338325
doi: 10.1002/jsfa.12797
doi:

Substances chimiques

Angiotensin-Converting Enzyme Inhibitors 0
Soybean Proteins 0
Peptides 0
Peptide Hydrolases EC 3.4.-
Endopeptidases EC 3.4.-
Metalloproteases EC 3.4.-
Angiotensins 0
Peptidyl-Dipeptidase A EC 3.4.15.1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

7153-7163

Subventions

Organisme : National Natural Science Foundation of China
ID : U2006205
Organisme : National Natural Science Foundation of China
ID : 32200021

Informations de copyright

© 2023 Society of Chemical Industry.

Références

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Auteurs

Xia Zhang (X)

State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.

Wen-Xiao Zhao (WX)

State Key Laboratory of Microbial Technology, Marine Biotechnology Center, Shandong University, Qingdao, China.

Yan Wang (Y)

State Key Laboratory of Microbial Technology, Marine Biotechnology Center, Shandong University, Qingdao, China.

Jun-Hui Cheng (JH)

Institute of Biochemical Engineering, College of Materials Science and Engineering, Qingdao University, Qingdao, China.

Kai Bao (K)

School of Life Sciences, Hubei University, Wuhan, China.

Jin He (J)

State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.

Xiu-Lan Chen (XL)

State Key Laboratory of Microbial Technology, Marine Biotechnology Center, Shandong University, Qingdao, China.

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Classifications MeSH