Variation in kinetic properties of cassava leaf β-glucosidases

Variations in kinetic properties of β-glucosidases from 16 cassava cultivars were osberved, in particular the K m values for p- nitrophenyl-β- d-glucoside and linamarin, K i for glucono-l,5-lactone and energy of activation. With the exception of p- nitrophenyl-β- d-glucoside , the cassava enzymes sh...

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Bibliographic Details
Published in:Biochemical systematics and ecology 1988-01, Vol.16 (6), p.525-528
Main Author: Yeoh, Hock-hin
Format: Article
Language:English
Subjects:
beta-glucosidase
Biological and medical sciences
cassava
cultivars
enzyme activity
Euphorbiaceae
Fundamental and applied biological sciences. Psychology
kinetics
leaves
linamarase
Manihot esculenta
Plant cytology, morphology, systematics, chorology and evolution
Spermatophyta
Systematics (diagnosis, chromosome numbers)
β-glucosidase
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Summary:Variations in kinetic properties of β-glucosidases from 16 cassava cultivars were osberved, in particular the K m values for p- nitrophenyl-β- d-glucoside and linamarin, K i for glucono-l,5-lactone and energy of activation. With the exception of p- nitrophenyl-β- d-glucoside , the cassava enzymes showed better hydrolytic activity towards their natural substrate, linamarin, than for salicin, prunasin and amygdalin. Ward's minimum variance cluster analyses of the data revealed potential systematic application.
ISSN:0305-1978
1873-2925
DOI:10.1016/0305-1978(88)90057-9