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Impact of Arg210-Ser211 deletion on thermostability of a truncated Bacillus sp. strain TS-23 α-amylase

Paper ID Volume ID Publish Year Pages File Format Full-Text
35639 45099 2008 7 PDF Available
Title
Impact of Arg210-Ser211 deletion on thermostability of a truncated Bacillus sp. strain TS-23 α-amylase
Abstract

One deletion mutant was constructed from the structural gene of a truncated Bacillus sp. strain TS-23 α-amylase (BACΔNC) by site-directed mutagenesis. BACΔNC and BACΔNC/ΔR210-S211 were overexpressed in recombinant Escherichia coli M15 cells and purified to nearly homologous by nickel-chelate chromatography. BACΔNC and BACΔNC/ΔR210-S211 were very similar with respect to specific activity, kinetic parameters, pH–activity profile, and temperature–activity curve. An increased half-life at 70 °C was observed for BACΔNC/ΔR210-S211, suggesting that Arg210-Ser211 deletion leads to a conformational change of the enzyme. Tryptophan emission fluorescence and circular dichroism spectra were nearly identical for the wild-type enzyme and BACΔNC/ΔR210-S211, but they showed a different sensitivity towards temperature-induced denaturation. These results indicated that the rigidity of the enzyme has been altered by Arg210-Ser211 deletion.

Keywords
Bacillus sp. TS-23; α-Amylase; Residue deletion; Thermostability; Circular dichroism
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Impact of Arg210-Ser211 deletion on thermostability of a truncated Bacillus sp. strain TS-23 α-amylase
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 5, May 2008, Pages 559–565
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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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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