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Substrate specificity of a galactose 6-phosphate isomerase from Lactococcus lactis that produces d-allose from d-psicose

Paper ID Volume ID Publish Year Pages File Format Full-Text
25149 43555 2007 8 PDF Available
Title
Substrate specificity of a galactose 6-phosphate isomerase from Lactococcus lactis that produces d-allose from d-psicose
Abstract

We purified recombinant galactose 6-phosphate isomerase (LacAB) from Lactococcus lactis using HiTrap Q HP and Phenyl-Sepharose columns. The purified LacAB had a final specific activity of 1.79 units/mg to produce d-allose. The molecular mass of native galactose 6-phosphate isomerase was estimated at 135.5 kDa using Sephacryl S-300 gel filtration, and the enzyme exists as a hetero-octamer of LacA and LacB subunits. The activity of galactose 6-phosphate isomerase was maximal at pH 7.0 and 30 °C, and enzyme activity was independent of metal ions. When 100 g/L of d-psicose was used as the substrate, 25 g/L of d-allose and 13 g/L of d-altrose were simultaneously produced at pH 7.0 and 30 °C after 12 h of incubation. The enzyme had broad specificity for various aldoses and ketoses. The interconversion of sugars with the same configuration except at the C2 position was driven by using a large amount of enzyme in extended reactions. The interconversion occurred via two isomerization reactions, i.e., the interconversion of d-allose ↔ d-psicose ↔ d-altrose, and d-allose to d-psicose reaction was faster than d-altrose to d-psicose reaction.

Keywords
Substrate specificity; d-Allose; d-Psicose; Isomerization; Galactose 6-phospate isomerase; Lactococcus lactis
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Substrate specificity of a galactose 6-phosphate isomerase from Lactococcus lactis that produces d-allose from d-psicose
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 132, Issue 1, 15 October 2007, Pages 88–95
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