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Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria

Paper ID Volume ID Publish Year Pages File Format Full-Text
34372 45020 2014 8 PDF Available
Title
Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria
Abstract

•The N-terminal sequence suggests novelty of the enzyme.•The purified protease has optimal temperature of 50 °C, optimal pH 10.0.•The NaCl dependent shift in temperature optima from 50 to 80 °C.•Structure and Function analysis of the enzyme by CD spectroscopy and FTIR.•SDS labile but surfactant and detergent stable and 95% stability in various surfactants and detergents even after 24 h.

An extracellular protease from a newly isolated seawater haloalkaliphilic bacterium, haloalkaliphilic bacteria Ve2-20-91 [HM047794], was purified and characterized. The enzyme is a monomer with a 37.2 kDa estimated molecular weight. It catalyzed reactions in the pH range 8–11 and performed optimally at pH 10. While maximal activity occurred at 50 °C, the temperature profile shifted from 50 to 80 °C in 1–3 M NaCl. The enzyme's thermal stability was probed using circular dichroism (CD) spectroscopy with NaCl at 50 and 70 °C. The changes in the enzyme's secondary structure were also analyzed using Fourier transform infrared spectroscopy (FTIR). The N-terminal amino acid sequence GKDGPPGLCGFFGCI exhibited low homology with other bacterial proteases, which highlights the enzyme's novelty. The enzyme was labile in anionic surfactant (1% w/v SDS) but showed stability in non-ionic surfactants (Tween 20, Tween 80 and Triton X-100 all 1% v/v), commercial detergents, and oxidizing and reducing agents. The enzyme's excellent stability in commercial detergents highlights its potential as a detergent additive.

Keywords
Alkaline protease; Detergent stability; Haloalkaliphilic bacteria; N-terminal sequence; CD spectroscopy; FTIR
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Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 6, June 2014, Pages 955–962
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
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us