Screening and characterization of proteases produced by deep-sea cold seep bacteria

Chenchen GUO; Chaomin SUN; Shimei WU

doi:10.1007/s00343-021-0441-2

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Screening and characterization of proteases produced by deep-sea cold seep bacteria

Biology | Updated：2023-05-20

- Screening and characterization of proteases produced by deep-sea cold seep bacteria
- Journal of Oceanology and Limnology Vol. 40, Issue 2, Pages: 678-689(2022)
- Affiliations：
  
  1.College of Life Sciences, Qingdao University, Qingdao 266071, China
  2.CAS Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
- Author bio：
  
  Shimei WU, E-mail: shimeiwu2016@126.com
- Funds：
- DOI：10.1007/s00343-021-0441-2
  CLC：
- Received：20 November 2020，
  
  Accepted：27 February 2021，
  
  Online First：30 April 2021，
  
  Published：2022-03
- Accepted：
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Chenchen GUO, Chaomin SUN, Shimei WU. Screening and characterization of proteases produced by deep-sea cold seep bacteria[J]. Journal of Oceanology and Limnology, 2022, 40(2): 678-689.
DOI：

Chenchen GUO, Chaomin SUN, Shimei WU. Screening and characterization of proteases produced by deep-sea cold seep bacteria[J]. Journal of Oceanology and Limnology, 2022, 40(2): 678-689. DOI： 10.1007/s00343-021-0441-2.

摘要

Abstract

Fifty protease-producing strains were screened from sediment of deep-sea cold seep

and divided into four different categories:

Bacillus

Pseudoalteromonas

Vibrio

and

Alteromonas

according to the sequences of 16s rRNA. Their abilities to produce protease

amylase

and lipase were determined

and a

Bacillus

strain gcc-1 displayed very strong alkaline protease activity and stability under different thermal and acidic conditions. The purification of the protease produced by strain gcc-1 was carried out by precipitation with ammonium sulfate

and sequentially chromatographed by anion exchange column and gel filtration. The purified protease showed a single band at the molecular weight of 28 kDa by SDS-PAGE. The characterization results show that the purified protease exhibited a considerable activity and stability in a wide thermal range of 10-80℃ and a wide acidic range of pH 6.5-11.5

and displayed highest activity at 40℃ and pH 8.5. Notably

the protease still maintained high activity even at low to 10℃. Furthermore

the protease exhibited good stability in presence of different surfactants

organic solvents

oxidizing agent H

and commercial detergents. Therefore

the protease produced by gcc-1 is a cold active and high stable enzyme

and has a promising potential in laundry detergent as an additive.

关键词

Keywords

references

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