کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
36443 | 45133 | 2005 | 5 صفحه PDF | دانلود رایگان |

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.
Journal: Process Biochemistry - Volume 40, Issue 8, July 2005, Pages 2597–2601