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Peptide synthesis in neat organic solvents with novel thermostable proteases

Paper ID Volume ID Publish Year Pages File Format Full-Text
16919 42622 2015 9 PDF Available
Title
Peptide synthesis in neat organic solvents with novel thermostable proteases
Abstract

•Novel thermostable subtilases were expressed in Escherichia coli.•Anhydrous enzyme prepared for use in organic solvents.•Efficient peptide bond formation in organic solvent mixtures.•Resistant to DMF as a peptide solubilizing agent.

Biocatalytic peptide synthesis will benefit from enzymes that are active at low water levels in organic solvent compositions that allow good substrate and product solubility. To explore the use of proteases from thermophiles for peptide synthesis under such conditions, putative protease genes of the subtilase class were cloned from Thermus aquaticus and Deinococcus geothermalis and expressed in Escherichia coli. The purified enzymes were highly thermostable and catalyzed efficient peptide bond synthesis at 80 °C and 60 °C in neat acetonitrile with excellent conversion (>90%). The enzymes tolerated high levels of N,N-dimethylformamide (DMF) as a cosolvent (40–50% v/v), which improved substrate solubility and gave good conversion in 5+3 peptide condensation reactions. The results suggest that proteases from thermophiles can be used for peptide synthesis under harsh reaction conditions.

Keywords
Thermostable; Thermophile; Protease; Subtilase; Organic solvent; Peptide synthesis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volumes 73–74, June 2015, Pages 20–28
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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