Elaine Mankge Malese, Penistacia Maela Mehabo, Mark Abrahams Adrian, Hope Serepa-Dlamini Mahloro
Department of Biotechnology and Food Technology, Faculty of Science, University of Johannesburg, Doornfontein Campus, PO Box 17011, Doornfontein, Johannesburg, 2028, South Africa.
Heliyon. 2024 May 4;10(9):e30736. doi: 10.1016/j.heliyon.2024.e30736. eCollection 2024 May 15.
Research on proteases and secondary metabolites from endophytes is an area that requires attention from researchers. In this study, proteases from sp. strain MHSD16 and sp. strain MHSD17 endophytes were characterised, and their potential biotechnological applications were investigated. Optimum protease production was achieved when isolates were grown in media containing (g/L): glucose 10g, casein 5g, yeast extract 5g, KHPO 2g, NaCO 10g at pH 9. The crude protease extracts were active in alkaline environments, thus referred to as alkaline proteases with optimal pH of 10. Additionally, sp. strain MHSD 16 and sp. strain MHSD17 proteases were active at high temperatures, with optimum enzyme activity at 50 °C. Thermostability profiles of these proteases showed that the enzymes were highly stable between (40-60 °C), maintaining over 85 % stability after 120 min incubation at 60 °C. Furthermore, the enzymes were stable and compatible with various household and laundry detergents. In the presence of commercial laundry detergent, OMO® 68 % and 72 % activity was retained for sp. strain MHSD16 and sp. strain MHSD17, respectively, while 67 % and 68 % activity were retained in the presence of Sunlight®. The potential application for use in detergents was investigated through the removal of blood stains with the crude alkaline extracts displaying efficient stain removal abilities. Feather degradation was also investigated and sp. MHSD17 exhibited feather keratin degrading properties more effectively than sp. MHSD16.
对内生菌的蛋白酶和次生代谢产物的研究是一个需要研究人员关注的领域。在本研究中,对来自sp.菌株MHSD16和sp.菌株MHSD17内生菌的蛋白酶进行了表征,并研究了它们潜在的生物技术应用。当分离株在含有(克/升):葡萄糖10克、酪蛋白5克、酵母提取物5克、KHPO 2克、NaCO 10克,pH值为9的培养基中生长时,可实现蛋白酶的最佳产量。粗蛋白酶提取物在碱性环境中具有活性,因此被称为碱性蛋白酶,最佳pH值为10。此外,sp.菌株MHSD 16和sp.菌株MHSD17的蛋白酶在高温下具有活性,最佳酶活性温度为50°C。这些蛋白酶的热稳定性曲线表明,这些酶在(40 - 60°C)之间高度稳定,在60°C孵育120分钟后保持超过85%的稳定性。此外,这些酶稳定且与各种家用和洗衣洗涤剂兼容。在商业洗衣洗涤剂存在的情况下,sp.菌株MHSD16和sp.菌株MHSD17分别保留了68%和72%的活性,而在Sunlight®存在的情况下保留了67%和68%的活性。通过用粗碱性提取物去除血渍来研究其在洗涤剂中的潜在应用,该提取物显示出有效的去污能力。还研究了羽毛降解情况,sp. MHSD17比sp. MHSD16更有效地表现出羽毛角蛋白降解特性。