Loading…
Improvement of branched-chain amino acid production by isolated high-producing protease from Bacillus amyloliquefaciens NY130 on isolated soy/whey proteins and their muscle cell protection
Branched-chain amino acids (BCAAs) are vital components of human and animal nutrition that contribute to the building blocks of proteins. In this study, 170 protease-producing strains were isolated and screened from soy-fermented foods. Bacillus amyloliquefaciens NY130 was obtained from Cheonggukjan...
Saved in:
Published in: | Food chemistry 2024-08, Vol.450, p.139327-139327, Article 139327 |
---|---|
Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Branched-chain amino acids (BCAAs) are vital components of human and animal nutrition that contribute to the building blocks of proteins. In this study, 170 protease-producing strains were isolated and screened from soy-fermented foods. Bacillus amyloliquefaciens NY130 was obtained from Cheonggukjang with high production of BCAAs. Optimal production of protease from B. amyloliquefaciens NY130 (protease NY130) was achieved at 42 °C and pH 6.0 for 21 h. It was purified and determined as 27- and 40 kDa. Protease NY130 showed maximum activity at pH 9.0 and 45 °C with Km value of 10.95 mg for ISP and 1.69 mg for WPI. Protease-treated ISP and WPI showed increased sweetness and saltiness via electronic tongue analysis and enhanced the protective effect against oxidative stress in C2C12 myocytes by increasing p-mTOR/mTOR protein expression to 160%. This work possesses potential in producing BCAAs by using protease for utilization in food.
[Display omitted]
•170 protease-producing strains were isolated and screened from soybean fermented foods.•Protease from Bacillus amyloliquefaciens NY130 with high production of BCAAs was characterized.•The optimized pH and temperature of purified protease were obtained at 9.0 and 45 °C.•The organoleptic properties of protease-treated ISP or WPI were changed.•Protease-treated ISP/WPI inhibited myostatin expression but enhanced p-mTOR/mTOR expression. |
---|---|
ISSN: | 0308-8146 1873-7072 |
DOI: | 10.1016/j.foodchem.2024.139327 |