Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis.

Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis. Research Abstract Details 

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Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis. Abstract Text:

Min Zhang,Cong Zhao,Lianxiang Du,Fuping Lu,Chen Gao,Min Zhang,Cong Zhao,LianXiang Du,FuPing Lu,Chen Gao,

The gene coding for a thermophilic neutral protease from Bacillus stearothermophilus was expressed in Bacillus subtilis DB104, under the control of the sacB gene promoter. This was followed by either the native signal peptide sequence of this protease or the signal peptide sequence of the sacB gene. The protease was purified 3.8-fold, with a specific activity of 16530 U mg(-1). As analyzed by SDS-PAGE, the molecular mass of the expressed protease was about 35 kDa, and the optimal temperature and pH of the protease were 65 degrees C and 7.5, respectively. Moreover, it still had about 80% activity after 1 h reaction at 65 degrees C.

Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis. Publishing Authors By Initials

M Zhang,C Zhao,L Du,F Lu,C Gao,M Zhang,C Zhao,L Du,F Lu,C Gao,

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Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Science in China. Series C, Life sciences / Chines

VOLUME: 51

Page Numbers: 52-9

Journal Abbreviation: Sci. China, C, Life Sci.

ISSN: 1006-9305

DAY: 7

MONTH: Feb

YEAR: 2008

Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis. Information

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LANGUAGE: eng

NlmUniqueID: 9611809

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Grant and Affiliation Information for Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis.

AFFILIATION: College of Engineering, Shenyang Agricultural University, Shenyang, 110161, China.

Country: China

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MEDLINETA: Sci China C Life Sci

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