000			01530nam a2200301Ia 4500
003			MX-MdCICY
005			20250625140655.0
040			_cCICY
090			_aB-11695
245	1	0	_aNovozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports
490	0		_vJournal of Molecular Catalysis B: Enzymatic, 57(1-4), p.171-176, 2009
520	3		_aThis paper shows that the properties of lipase B fromCandida antarctica (CAL-B)may be easily modulated using different hydrophobic supports to immobilize it (octyl and butyl-agarose, octadecyl-Sepabeads or Lewatit). CAL-B could be fully desorbed from the supports by just incubating the biocatalyst with Triton X-100, although the concentration of detergent necessary was to fully desorb the enzyme varied with the support employed (from 1
650	1	4	_aLEWATIT
650	1	4	_aINTERFACIAL ACTIVATION OF LIPASES
650	1	4	_aENANTIOSELECTIVITY
650	1	4	_aHYDROPHOBIC SUPPORTS
650	1	4	_aMODULATION OF ENZYME PROPERTIES
650	1	4	_aMANDELIC ACID
650	1	4	_a3-PHENYLGLUTARIC ACID DIMETHYL DIESTER
700	1	2	_aCabrera, Z.
700	1	2	_aFernandez-Lorente, G.
700	1	2	_aFernandez-Lafuente, G.
700	1	2	_aPalomo, J.M.
700	1	2	_aGuisan, J.M.
856	4	0	_uhttps://drive.google.com/file/d/1uX-tB3k0FC8srmULNl_NHLDpcxeJYlgy/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942			_2Loc _cREF1
008			250602s9999 xx |||||s2 |||| ||und|d
999			_c45911 _d45911