Tungsten 1995

A novel L‐pantolactone hydrolase, Lph, from Agrobacterium tumefaciens Lu681 was characterized, which stereospecifically hydrolyses L‐pantolactone to L‐pantoic acid yielding D‐pantolactone with > 95% enantiomeric excess. The enzyme was found to be a 30 kDa‐Zn2+‐hydrolase with a Km for L‐pantolactone of 7 mM and a Vmax of 30 U/mg. The corresponding lph gene was identified as an 807 bp ORF and cloned into E. coli. It was overexpressed under control of Ptac and Prha yielding enzyme activities of up to 600 U/g dry weight. Resolution of d,l‐pantolactone in repeated batches with isolated Lph and enzyme recovery by membrane filtration gave D‐pantolactone with 50% yield and 90–95% ee over 6 days. Covalent immobilization to EupergitC led to a stable biocatalyst easy to handle in a repeated batch production of D‐pantolactone. Further improvements in the activity of Lph were achieved by directed evolution of the enzyme. Activities of mutants F62S, K197D and F100L were increased 2.3, 1.7, and 1.5 fold, respectively.

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ChemInform Abstract: Tungsten 1995

WONG¹

1998

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Tungsten 1995

Cited by 12 publications

References 191 publications

Enzymes

Enzymes

Development of a Novel Biocatalyst for the Resolution ofrac-Pantolactone

ChemInform Abstract: Tungsten 1995

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