Properties of recombinant Rhizomucor miehei lipase with amino acid substitutions of Phe94 in the substrate binding domain

Properties of recombinant Rhizomucor miehei lipase with amino acid substitutions of Phe94 in the substrate binding domain

The chain length specificity of Rhizomucor miehei lipase was altered by substituting Phe94 in the protein groove which is responsible for accommodating the acyl chain of the substrate. Three recombinant enzymes, Phe94Arg, Phe94Glu and Phe94Gln, were expressed in Pichia pastoris, purified and their a...

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Veröffentlicht in:Biotechnology letters 2001-04, Vol.23 (7), p.563-568
Hauptverfasser: OH, Si-Won, GASKIN, Duncan J. H, DAE YOUNG KWON, VULFSON, Evgeny N
Format: Artikel
Sprache:eng
Schlagworte:
Amino acids
Biological and medical sciences
Biotechnology
Enzymes
Esters
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Microbiology
p-nitrophenyl esters
Protein engineering
Rhizomucor miehei
triacylglycerol
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Zusammenfassung:The chain length specificity of Rhizomucor miehei lipase was altered by substituting Phe94 in the protein groove which is responsible for accommodating the acyl chain of the substrate. Three recombinant enzymes, Phe94Arg, Phe94Glu and Phe94Gln, were expressed in Pichia pastoris, purified and their ability to hydrolyse p-nitrophenyl esters and triacylglycerols of different chain length was studied.[PUBLICATION ABSTRACT]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1010308824956