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Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production.
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.
Afiliação
  • Doan CT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Tran TN; Department of Chemistry, Tamkang University, New Taipei City 25137, Taiwan.
  • Nguyen MT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Nguyen HK; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Tran TKT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Nguyen TH; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Tran TPH; Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Nguyen VB; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Nguyen AD; Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • Wang SL; Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
Polymers (Basel) ; 14(13)2022 Jul 05.
Article em En | MEDLINE | ID: mdl-35808786
ABSTRACT
This study attempted to use fishery processing wastes to produce protease by Paenibacillus elgii 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% K2HPO4, 0.073% MgSO4, 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 P. elgii 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. P. elgii TKU051 protease was strongly inhibited by ethylenediaminetetraacetic acid and 1,10-phenanthroline, indicating its precise metalloprotease property. P. elgii 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 P. elgii TKU051 protease could improve the free-radical scavenging activity of fishery wastes. In short, P. elgii TKU051 has potential application in eco-friendly approaches to efficiently convert fishery wastes to metalloprotease.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2022 Tipo de documento: Article