Proteolysin, a Novel Highly Thermostable and Cosolvent-Compatible Protease from the Thermophilic Bacterium Coprothermobacter proteolyticus

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Proteolysin, a novel highly thermostable and cosolvent-compatible protease from the thermophilic bacterium Coprothermobacter proteolyticus.

Through genome mining, we identified a gene encoding a putative serine protease of the thermitase subgroup of subtilases (EC 3.4.21.66) in the thermophilic bacterium Coprothermobacter proteolyticus. The gene was functionally expressed in Escherichia coli, and the enzyme, which we called proteolysin, was purified to near homogeneity from crude cell lysate by a single heat treatment step. Proteol...

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Proteolysin , a Novel Highly Thermostable and Cosolvent - Compatible 1 Protease from the Thermophilic Bacterium

# Corresponding author. Mailing address: Biotransformation and Biocatalysis, 18 Groningen Biomolecular Science and Biotechnology Institute, University of 19 Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands. E-mail: 20 [email protected]. Phone: +31-50-3634008; Fax: +31-50-3634165. 21 Copyright © 2013, American Society for Microbiology. All Rights Reserved. Appl. Environ. Microbiol. d...

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Protease Complement of the Thermophilic Bacterium Coprothermobacter proteolyticus

Thermal bacteria that live in higher temperature have been considered as good candidates for bioremediation and processing of protein-rich wastewater. However, very little is known about the proteases, the enzymes that digest the protein wastes in these organisms. In this study, we present a comparative genomic analysis of the protease complement in a thermal bacterium Coprothermobacter proteol...

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Expression and Characterization of Coprothermobacter proteolyticus Alkaline Serine Protease

A putative protease gene (aprE) from the thermophilic bacterium Coprothermobacter proteolyticus was cloned and expressed in Bacillus subtilis. The enzyme was determined to be a serine protease based on inhibition by PMSF. Biochemical characterization demonstrated that the enzyme had optimal activity under alkaline conditions (pH 8-10). In addition, the enzyme had an elevated optimum temperature...

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Expression and characterization of recombinant thermostable alkaline phosphatase from a novel thermophilic bacterium Thermus thermophilus XM.

A gene (tap) encoding a thermostable alkaline phosphatase from the thermophilic bacterium Thermus thermophilus XM was cloned and sequenced. It is 1506 bp long and encodes a protein of 501 amino acid residues with a calculated molecular mass of 54.7 kDa. Comparison of the deduced amino acid sequence with other alkaline phosphatases showed that the regions in the vicinity of the phosphorylation s...

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ژورنال

عنوان ژورنال: Applied and Environmental Microbiology

سال: 2013

ISSN: 0099-2240,1098-5336

DOI: 10.1128/aem.01479-13