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Characterization of Bacillus kaustophilus leucine aminopeptidase immobilized in Ca-alginate/k-carrageenan beads

Paper ID Volume ID Publish Year Pages File Format Full-Text
4638 235 2008 7 PDF Available
Title
Characterization of Bacillus kaustophilus leucine aminopeptidase immobilized in Ca-alginate/k-carrageenan beads
Abstract

Properties of Bacillus kaustophilus leucine aminopeptidase (BkLAP) immobilized by entrapment in Ca-alginate/k-carrageenan hydrogel were examined. For the free and immobilized BkLAP, optimum pH was found to be 8.0 and 7.5, respectively. The optimum temperature of the free and immobilized enzymes was also observed to be 55 and 60 °C, respectively. Thermal stability of BkLAP was increased as a result of immobilization. Maximum reaction rate (Vmax) and Michalis–Menten constant (Km) of BkLAP were changed significantly upon immobilization. The immobilized enzyme could be reused at least up to 10 cycles without any further loss of activity. After incubating at 4 °C for 30 days, the stability values for the immobilized enzyme system were found to be 90%. In the presence of 50 mM H2O2, the immobilized BkLAP was more stable respective to the free enzyme, indicating that the oxidative stability of the enzyme can be improved by immobilization.

Keywords
Leucine aminopeptidase; Bacillus kaustophilus; Immobilization; Alginate; k-Carrageenan; Stability
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Characterization of Bacillus kaustophilus leucine aminopeptidase immobilized in Ca-alginate/k-carrageenan beads
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 39, Issue 2, 15 April 2008, Pages 376–382
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