Improvement of the Thermostability of Pyruvate Decarboxylase by Modification with an Amylose Derivative

Pyruvate decarboxylase from brewer's yeast was modified with the N-hydroxysuccinimide ester of an amylose glycylglycine adduct and some properties of the resulting conjugate were studied with regard to thermostability. By this conjugation the optimum temperature of the activity of pyruvate deca...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1995, Vol.59 (8), p.1581-1583
Hauptverfasser:	Ohba, Hideki, Yasuda, Seiji, Hirosue, Hideharu, Yamasaki, Nobuyuki
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Biotechnology Chemical synthesis for preparing modified enzymes, enzyme fragments and enzyme analogs Enzyme engineering Fundamental and applied biological sciences. Psychology Methods. Procedures. Technologies Production of selected enzymes
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Beschreibung
Zusammenfassung:	Pyruvate decarboxylase from brewer's yeast was modified with the N-hydroxysuccinimide ester of an amylose glycylglycine adduct and some properties of the resulting conjugate were studied with regard to thermostability. By this conjugation the optimum temperature of the activity of pyruvate decarboxylase shifted from 35°C to 40°C. The conjugate showed a greater resistance than the enzyme to inactivating by heat treatment. It is suggested that AG-ONSu can be advantageously used for stabilization of the thermolabile enzyme.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.59.1581