Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341

Quan Fu Wang; Jin Lai Miao; Yan Hua Hou; Yu Ding; Guo Dong Wang; Guang You Li

doi:10.1007/s10529-005-0016-x

Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341

Quan Fu Wang
, Jin Lai Miao^*
, Yan Hua Hou
, Yu Ding
, Guo Dong Wang
, Guang You Li

^*Corresponding author for this work

Ocean University of China
Ministry of Natural Resources of the People's Republic of China
Harbin Institute of Technology Weihai

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5-12 with maximum activity at 35°C (assayed over 10 min). Activity at 0°C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.

Original language	English
Pages (from-to)	1195-1198
Number of pages	4
Journal	Biotechnology Letters
Volume	27
Issue number	16
DOIs	https://doi.org/10.1007/s10529-005-0016-x
State	Published - Aug 2005
Externally published	Yes

Keywords

Antarctic
Cold-active serine protease
Colwellia
Psychrophilic bacteria

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10.1007/s10529-005-0016-x

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title = "Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341",

abstract = "Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5-12 with maximum activity at 35°C (assayed over 10 min). Activity at 0°C was nearly 30\% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.",

keywords = "Antarctic, Cold-active serine protease, Colwellia, Psychrophilic bacteria",

author = "Wang, \{Quan Fu\} and Miao, \{Jin Lai\} and Hou, \{Yan Hua\} and Yu Ding and Wang, \{Guo Dong\} and Li, \{Guang You\}",

year = "2005",

month = aug,

doi = "10.1007/s10529-005-0016-x",

language = "英语",

volume = "27",

pages = "1195--1198",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

number = "16",

}

TY - JOUR

T1 - Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341

AU - Wang, Quan Fu

AU - Miao, Jin Lai

AU - Hou, Yan Hua

AU - Ding, Yu

AU - Wang, Guo Dong

AU - Li, Guang You

PY - 2005/8

Y1 - 2005/8

N2 - Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5-12 with maximum activity at 35°C (assayed over 10 min). Activity at 0°C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.

AB - Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5-12 with maximum activity at 35°C (assayed over 10 min). Activity at 0°C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.

KW - Antarctic

KW - Cold-active serine protease

KW - Colwellia

KW - Psychrophilic bacteria

UR - https://www.scopus.com/pages/publications/24744444056

U2 - 10.1007/s10529-005-0016-x

DO - 10.1007/s10529-005-0016-x

M3 - 文章

C2 - 16158263

AN - SCOPUS:24744444056

SN - 0141-5492

VL - 27

SP - 1195

EP - 1198

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 16

ER -

Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341

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Keywords

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