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利用渔业废弃物进行液体发酵生产金属蛋白酶的潜力。

Potential of the Liquid Fermentation of Fishery Waste by for Metalloprotease Production.

作者信息

Doan Chien Thang, Tran Thi Ngoc, Nguyen Minh Trung, Nguyen Huu Kien, Tran Thi Kim Thi, Nguyen Thi Hanh, Tran Thi Phuong Hanh, Nguyen Van Bon, Nguyen Anh Dzung, Wang San-Lang

机构信息

Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.

Department of Chemistry, Tamkang University, New Taipei City 25137, Taiwan.

出版信息

Polymers (Basel). 2022 Jul 5;14(13):2741. doi: 10.3390/polym14132741.

Abstract

This study attempted to use fishery processing wastes to produce protease by TKU051. Of the tested wastes, tuna head powder (THP) was found to be the most effective carbon and nitrogen (C/N) source, and the optimal conditions were as follows: 0.811% THP, 0.052% KHPO, 0.073% MgSO, initial pH of 8.96, incubation temperature of 31.4 °C, and incubation time of 3.092 days to achieve the maximum protease activity of 2.635 ± 0.124 U/mL. A protease with a molecular weight of 29 kDa was purified and biochemically characterized. Liquid chromatography with tandem mass spectrometry analysis revealed an amino acid sequence of STVHYSTR of TKU051 protease, suggesting that the enzyme may belong to the M4 family of metalloproteases. The optimal activity of the enzyme was achieved at 60 °C and pH 8. TKU051 protease was strongly inhibited by ethylenediaminetetraacetic acid and 1,10-phenanthroline, indicating its precise metalloprotease property. TKU051 protease displayed the activity toward casein and raw fishery wastes such as tuna heads, tuna viscera, shrimp heads, and squid pens. Finally, the purified TKU051 protease could improve the free-radical scavenging activity of fishery wastes. In short, TKU051 has potential application in eco-friendly approaches to efficiently convert fishery wastes to metalloprotease.

摘要

本研究试图利用渔业加工废料通过菌株TKU051生产蛋白酶。在测试的废料中,金枪鱼鱼头粉(THP)被发现是最有效的碳氮(C/N)源,最佳条件如下:0.811% THP、0.052% KHPO、0.073% MgSO、初始pH值8.96、培养温度31.4℃、培养时间3.092天,以达到最大蛋白酶活性2.635±0.124 U/mL。纯化了一种分子量为29 kDa的蛋白酶并对其进行了生化特性分析。液相色谱串联质谱分析揭示了TKU051蛋白酶的氨基酸序列为STVHYSTR,表明该酶可能属于金属蛋白酶的M4家族。该酶在60℃和pH 8时达到最佳活性。TKU051蛋白酶受到乙二胺四乙酸和1,10-菲咯啉的强烈抑制,表明其具有确切的金属蛋白酶特性。TKU051蛋白酶对酪蛋白以及金枪鱼鱼头、金枪鱼内脏、虾头和鱿鱼笔等生渔业废料具有活性。最后,纯化的TKU051蛋白酶可以提高渔业废料的自由基清除活性。简而言之,TKU051在将渔业废料高效转化为金属蛋白酶的环保方法中具有潜在应用价值。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79a9/9268979/c7c286102a57/polymers-14-02741-g002.jpg

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