Cargando…
Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production
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% K(2)HPO(4), 0.073%...
Autores principales: | , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9268979/ https://www.ncbi.nlm.nih.gov/pubmed/35808786 http://dx.doi.org/10.3390/polym14132741 |
_version_ | 1784744120063885312 |
---|---|
author | 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 |
author_facet | 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 |
author_sort | Doan, Chien Thang |
collection | PubMed |
description | 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% K(2)HPO(4), 0.073% MgSO(4), 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. |
format | Online Article Text |
id | pubmed-9268979 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-92689792022-07-09 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 Polymers (Basel) Article 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% K(2)HPO(4), 0.073% MgSO(4), 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. MDPI 2022-07-05 /pmc/articles/PMC9268979/ /pubmed/35808786 http://dx.doi.org/10.3390/polym14132741 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article 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 Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production |
title | Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production |
title_full | Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production |
title_fullStr | Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production |
title_full_unstemmed | Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production |
title_short | Potential of the Liquid Fermentation of Fishery Waste by Paenibacillus elgii for Metalloprotease Production |
title_sort | potential of the liquid fermentation of fishery waste by paenibacillus elgii for metalloprotease production |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9268979/ https://www.ncbi.nlm.nih.gov/pubmed/35808786 http://dx.doi.org/10.3390/polym14132741 |
work_keys_str_mv | AT doanchienthang potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT tranthingoc potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT nguyenminhtrung potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT nguyenhuukien potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT tranthikimthi potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT nguyenthihanh potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT tranthiphuonghanh potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT nguyenvanbon potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT nguyenanhdzung potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction AT wangsanlang potentialoftheliquidfermentationoffisherywastebypaenibacilluselgiiformetalloproteaseproduction |