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090			_aB-12861
245	1	0	_aKinetics and mechanism of heterogeneous hydrolysis of poly[(R)-3-hydroxybutyrate]fielm by PHA depolymerases
490	0		_vInt. J. Biol. Macromol., 15(6), p.361-366, 1993
520	3		_aThe kinetics and mechanism of enzymatic degradation on the surface of poly[(R)-3-hydroxybutyrate](PC(R)-3HB]) jilm have been studied using three types of extracellular poly(hydroxyalkanoate)(PHA)depolymerases from Alcaligenes faecalis, Pseudomonas pickettii and Comamonas testosteroni. The monomer and dimer of 3-hydroxybutyric acid were produced during the course of the enzymatic degradation of PC(R)-3HB]film, and the rate of production was determined by monitoring the increase in absorbance at 210 nm on a spectrophotometer. The rate of enzymatic degradation increased to a maximum value with the concentration of PHA depolymerase, followed by a gradual decrease. The kinetic data were accountedfor in terms of a heterogeneous enzymatic reaction, involving enzymatic degradation on the surface of PC(R)-3HB]jilm via two steps of adsorption and hydrolysis by a PHA depolymerase with binding and catalytic domains. The kinetic results suggest that the properties oj-the catalytic domains are very similar among the three PHA depolymerases, but that those of the binding domains are strongly dependent on the type of depolymerase.
650	1	4	_aENZYMATIC DEGRADATION
650	1	4	_aPHA DEPOLYMERASES
650	1	4	_aPOLY[(R)-3-HYDROXYBUTYRATE]
650	1	4	_aHETEROGENEOUS HYDROLYSIS
650	1	4	_aKINETIC MODEL
700	1	2	_aMukai, K.
700	1	2	_aYamada, K.
700	1	2	_aDoit, Y.
856	4	0	_uhttps://drive.google.com/file/d/13VXs7PmxOF3YZjJ9xswQ2fgDIC6LDAnA/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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