Year: 2024
Type: article
Abstract: BACKGROUND Bacillus subtilis AU‐2, isolated from the gut of Tribolium castaneum, was used for protease production. The purified protease was evaluated for its potential in food‐related applications including meat tenderization, milk coagulation, and the preparation of enzymatic soybean hydrolysates. Enzymatic hydrolysis of soy protein is an effective method for producing protein hydrolysates with optimal techno‐functional properties. RESULTS This study confirmed that B. subtilis AU‐2 is a commensal with T. castaneum, within the insect gut flora. The purified protease obtained from B. subtilis AU‐2 exhibited meat tenderization activity and an ability to promote milk coagulation within a 20 min timeframe. Soybean hydrolysate prepared using the protease exhibited a relatively higher degree of hydrolysis (20.1%) than pepsin, trypsin, and papain. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) peptide fragmentation pattern of the enzymatically prepared soy protein hydrolysate revealed the disappearance of ~35 kDa protein bands after 4 h protease treatment. The prepared soy protein hydrolysate showed improved emulsifying capacity (EC) (705 mL g−1) and exhibited significant 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) antioxidant activity (77.89%) and hydroxyl (OH) radical scavenging activity (97.23%). CONCLUSIONS The protease obtained from the newly isolated B. subtilis AU‐2 strain exhibited potential for food‐related applications, including meat tenderization, milk clotting, and soybean hydrolysate preparation. Its accessibility opens avenues for utilization in the food processing industry. © 2024 Society of Chemical Industry.
DOI: 10.1002/jsfa.14089
Authors: Santosh D. Raut, Vipul A. Bharuka, Aniketa R. Patel, Ulhas K. Patil
Language: English
Subfield: Biotechnology
Domain: Life Sciences
SDG: Zero hunger
Open Access status: bronze
OpenAlex ID: W4405763962