Screening and Characterization of Marine Bacillus atrophaeus G4 Protease and Its Application in the Enzymatic Hydrolysis of Sheep (Ovis aries) Placenta for the Preparation of Antioxidant Peptides
文献类型: 外文期刊
第一作者: Wang, Wei
作者: Wang, Wei;Peng, Guoqing;Sun, Jingjing;Jiang, Chengcheng;Hao, Jianhua;Hao, Jianhua;Zhang, Xiu
作者机构:
关键词:
protease;
期刊名称:MOLECULES ( 影响因子:4.6; 五年影响因子:5.0 )
ISSN:
年卷期: 2025 年 30 卷 10 期
页码:
收录情况: SCI
摘要: Proteolytic enzymes, which play a crucial role in peptide bond cleavage, are widely applied in various industries. In this study, protease-producing bacteria were isolated and characterized from marine sediments collected from the Yellow Sea, China. Comprehensive screening and 16S rDNA sequencing identified a promising G4 strain as Bacillus atrophaeus. Following meticulous optimization of fermentation conditions and medium composition via response surface methodology, protease production using strain G4 was significantly enhanced by 64%, achieving a yield of 3258 U/mL. The G4 protease exhibited optimal activity at 50 degrees C and pH 7.5, demonstrating moderate thermal stability with 52% residual activity after 30-min incubation at 50 degrees C-characteristics typical of an alkaline protease. Notably, the enzyme retained over 79% activity across a broad pH range (6-11) and exhibited excellent salt tolerance, maintaining over 50% activity in a saturated NaCl solution. Inhibition by phenylmethylsulfonyl fluoride, a serine protease inhibitor, confirmed its classification as a serine protease. The enzyme's potential in generating bioactive peptides was further demonstrated through hydrolysis of sheep (Ovis aries) placenta, resulting in a hydrolysate with notable antioxidant properties. The hydrolysate exhibited a 64% superoxide anion scavenging activity, surpassing that of reduced glutathione. These findings expand the current understanding of Bacillus atrophaeus G4 proteases and provide a foundation for innovative sheep placenta utilization with potential industrial applications.
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