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090			_aB-15525
245	1	0	_aDesigning cross-linked lipase aggregates for optimum performance as biocatalysts
490	0		_vBiocatalysis and Biotransformation, 26(3), p.235-242, 2008
520	3		_aCross-linked enzyme aggregates (CLEAs)are prepared by precipitation of an enzyme and then chemical cross-linking the precipitate. Three CLEAs of lipase with glutaraldehyde concentrations of 10 mM (CLEA A), 40 mM (CLEA B)and 60 mM (CLEA C)were prepared. Studies show that there is a trade-off between thermal stability vs transesterification/ hydrolysis rate vs enantioselectivity. The initial rates for transesterification of b-citronellol for the uncross-linked enzyme and CLEAs A, B and C were 243, 167, 102 and 40 mmol mg 1 h 1, respectively. Their thermal stabilities in aqueous media, as reflected by their half-life values at 558C, were 6, 9, 13 and 16 h, respectively. The enantioselectivity, E values (for kinetic resolution of b-citronellol by transesterification)were 19, 74, 11 and 6, respectively. These results show that CLEA C was the most thermostable; the uncross-linked enzyme was best at obtaining the highest transesterification rate; and CLEA A was best suited for the enantioselective synthesis. Scanning electron microscopy (SEM)showed that the morphology of CLEA was dependent upon the extent of cross-linking.
650	1	4	_aCROSS-LINKED ENZYME AGGREGATES
650	1	4	_aENANTIOSELECTIVITY
650	1	4	_aFAT SPLITTING, LIPASE
650	1	4	_aTRANSESTERIFICATION
650	1	4	_aTHERMAL STABILITY
700	1	2	_aMajumder, A.B.
700	1	2	_aMondal, K.
700	1	2	_aSingh, T.P.
700	1	2	_aGupta, M.N.
856	4	0	_uhttps://drive.google.com/file/d/1T5uIvHVDV5Ij_ws8EDpj5Jj8Vw9mTwvq/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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