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Purification and characterization of a thermostable protease from a newly isolated Geobacillus sp. YMTC 1049

Paper ID Volume ID Publish Year Pages File Format Full-Text
18252 42715 2007 6 PDF Available
Title
Purification and characterization of a thermostable protease from a newly isolated Geobacillus sp. YMTC 1049
Abstract

A thermostable extracellular protease named protease RH-1 was purified from a thermophilic Geobacillus sp. YMTC 1049 isolated from a hotspring in Rehai, Tengchong, Yunnan Province, China. Protease RH-1 was a serine protease since it was inhibited by 10 mM PMSF. It was a monomeric enzyme with molecular weight of 59.2 kDa. The protease showed the highest activity at 85 °C at pH 7.5 and was stable for 10.0 h at 65 °C. The activity of protease RH-1 was enhanced by 10 mM EDTA and EGTA. In addition, the activity of the protease can be activated by Ca2+ and Mg2+ but inhibited partially by Ba2+, Zn2+, Pb2+, Co2+, Mn2+ and Cu2+. It was noteworthy that protease RH-1 was resistant to denaturation by SDS, dithiothreitol, urea and guanidine hydrochloride (GdnHCl). Therefore, protease RH-1 was greatly different from those isolated from other strains of Geobacillus and may be applied in industrial processes that are performed under high temperature, in alkaline medium, or with the presence of denaturants.

Keywords
Geobacillus sp. YMTC 1049; Thermophilic protease RH-1; Thermostability; Denaturants
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Purification and characterization of a thermostable protease from a newly isolated Geobacillus sp. YMTC 1049
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 40, Issue 6, 2 May 2007, Pages 1592–1597
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us