Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, 3018, Sfax, Tunisia.
Laboratory of Microorganisms and Biomolecules (LMB), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, 3018, Sfax, Tunisia.
Environ Sci Pollut Res Int. 2020 May;27(13):15842-15855. doi: 10.1007/s11356-020-08076-w. Epub 2020 Feb 24.
The efficiency of the proteolytic strain Anoxybacillus kamchatkensis M1V in the fermentation of speckled shrimp by-product was investigated for the recovery of a deproteinized bioactive hydrolysate. The biological activities of the resulting hydrolysate were also examined by applying several antioxidant and enzyme inhibitory assays. The strain M1V was found to produce high level of protease activity (2000 U/mL) when grown in media containing only shrimp powder at 25 g/L. The crude protease displayed a significant deproteinization capabiliy, with the best efficiency (48%) being recorded for an enzyme to substrate (E/S) ratio of 30 U/mg. Following the deproteinization, chitin was recovered and the authenticity was confirmed by Fourier-transform infrared spectroscopy (FTIR) analysis. On the other hand, the obtained hydrolysate showed a significant enzymatic inhibitory potential against acetylcholinesterase, tyrosinase, amylase, and angiotensin I convertase, and a strong antioxidant activity. Graphical Abstract.
研究了蛋白酶产生菌卡玛切塔斯芽孢杆菌 M1V 在斑点虾副产物发酵中的效率，以回收一种去蛋白的生物活性水解产物。通过应用几种抗氧化和酶抑制测定法，还检查了所得水解产物的生物活性。当在仅含 25 g/L 虾粉的培养基中生长时，菌株 M1V 产生的蛋白酶活性（2000 U/mL）很高。粗蛋白酶显示出显著的脱蛋白能力，酶与底物（E/S）比为 30 U/mg 时记录到最佳效率（48%）。脱蛋白后，回收甲壳素，并通过傅里叶变换红外光谱（FTIR）分析确认其真实性。另一方面，所得水解产物对乙酰胆碱酯酶、酪氨酸酶、淀粉酶和血管紧张素 I 转换酶具有显著的酶抑制潜力，并且具有很强的抗氧化活性。
