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Production of pyruvate from lactate using recombinant Pichia pastoris cells as catalyst

Paper ID Volume ID Publish Year Pages File Format Full-Text
36443 45133 2005 5 PDF Available
Title
Production of pyruvate from lactate using recombinant Pichia pastoris cells as catalyst
Abstract

Because of the synergistic presence of enzyme systems, whole-cell biocatalysts are an advantageous means of oxidizing α-hydroxy to α-keto carboxylic acids. The effect of different parameters on conversion were determined when whole cells converted l-lactate to pyruvate. The biocatalyst was a double recombinant Pichia pastoris containing a glycolate oxidase and catalase enzyme system. A marked increase in conversion occurred with oxygen compared to air. This indicated that the oxygen concentration was an important factor in the rate-limiting step. Lactate concentrations above 0.5 M showed substrate inhibition. Although temperature played an important role in enzyme stability, whole-cell tranformants were much more stable over time than soluble enzymes.

Keywords
Glycolate oxidase; Lactate; Pichia pastoris; Pyruvic acid; α-Hydroxy carboxylic acids; α-Keto carboxylic acids
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Production of pyruvate from lactate using recombinant Pichia pastoris cells as catalyst
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 8, July 2005, Pages 2597–2601
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
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