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Stability and conformational changes of transglutaminase from Streptomyces hygroscopicus in ethanol–aqueous medium

Paper ID Volume ID Publish Year Pages File Format Full-Text
35538 45094 2008 5 PDF Available
Title
Stability and conformational changes of transglutaminase from Streptomyces hygroscopicus in ethanol–aqueous medium
Abstract

Effect of ethanol on the stability and conformational changes of transglutaminase from Streptomyces hygroscopicus (MTGase) was studied. The presence of 10% ethanol increased 20% activity and about 85% activity was lost in 50% ethanol–aqueous solution after incubation for 60 min at 25 °C. The Km and Vmax of the enzyme were 63.13 mmol/L and 14.02 μmol/(mg protein min) in the presence of 10% ethanol, and 34.20 mmol/L and 0.68 μmol/(mg protein min) in the presence of 30% ethanol, respectively. The results of spectral determination indicated that MTGase did not undergo significant structural changes in 10% ethanol–aqueous solution. At ethanol concentration of 40%, the α-helix structure content of the enzyme decreased from 20.5 ± 0.5% to 14.3 ± 0.7% and the unordered structure content increased from 46.4 ± 0.5% to 72.6 ± 1.7%. Some polyhydroxy compounds could improve the stability of the enzyme at high ethanol concentration.

Keywords
Microbial transglutaminase; Streptomyces hygroscopicus; Ethanol; Stability; Conformational changes; Polyols
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Stability and conformational changes of transglutaminase from Streptomyces hygroscopicus in ethanol–aqueous medium
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 8, August 2008, Pages 887–891
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
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Any Questions? feel free to contact us