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Evidence for a halotolerant-alkaline laccase in Streptomyces psammoticus: Purification and characterization

Paper ID Volume ID Publish Year Pages File Format Full-Text
35849 45110 2008 7 PDF Available
Title
Evidence for a halotolerant-alkaline laccase in Streptomyces psammoticus: Purification and characterization
Abstract

An unusual halotolerant-alkaline laccase from Streptomyces psammoticus has been purified to homogeneity through anion exchange and gel filtration chromatography steps with an overall purification fold of 12.1. The final recovery of the enzyme was 22.1%. The molecular mass of the purified laccase was about 43 kDa. The enzyme was active in the alkaline pH range with pH optima at 8.5 and 97% activity retention at pH 9.0. The optimum temperature was 45 °C. The enzyme was stable in the pH range 6.5–9.5 and up to 50 °C for 90 min. The enzyme was tolerant to NaCl concentrations up to 1.2 M. It was inhibited by all the putative laccase inhibitors while the enzyme was activated by metal ions like Fe, Zn, Cu, Na and Mg. Fe enhanced the enzyme activity by twofold (204%). The enzyme showed lowest Km value with pyrogallol (0.25 mM) followed by ABTS (0.39 mM). The purified enzyme was a typical blue laccase with an absorption peak at 600 nm.

Keywords
Laccase; Halotolerance; Alkaline enzyme; Purification; Characterization; Streptomyces psammoticus
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Evidence for a halotolerant-alkaline laccase in Streptomyces psammoticus: Purification and characterization
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 6, June 2008, Pages 654–660
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