Chemoenzymatic Kinetic resolution of (R)-malathion in aqueous media

BMC Chemistry

Table 1 Lipase-catalyzed enantioselective hydrolysis of racemic malathion at optimal conditions

Enzyme % - Temp °C	Candida rugosa lipase			Mucor javanicus lipase			Porcine pancreatic lipase
	C	ee _p	E	c	ee _p	E	c	ee _p	E
5-30	11.2	45.5	28	1.4	25.9	12	1.3	63.4	77
5-40	23.8	47.8	32	2.8	27.1	13	4.8	70.7	59
5-50	26.3	38.5	31	3.2	23.4	10	9.7	60.2	32
5-60	25.3	2.5	17	2.9	13.0	5	7.8	42.3	21
10-30	16.8	37.5	24	1.87	43.4	16	2.1	70.2	32
10-40	34.5	47.1	55	2.56	45.9	116	8.8	72.1	68
10-50	37.2	41.2	30	2.83	45.1	28	8.8	56.2	52
10-60	33.8	30.4	20	2.04	43.3	22	9.0	41.1	32
15-30	35.2	32.3	80	2.12	65.7	80	9.7	56.43	62
15-40	46.5	86.8	185	4.88	72.9	94	12.88	58.61	81
15-50	47.1	54.2	83	4.9	70.4	108	13.12	45.67	62
15-60	48.4	32.4	23	4.4	67.8	86	13.36	40.71	24

Experimental condition: phosphates buffer pH 7.2 as solvent, 40 °C, stirring at 250 rpm, reaction time 48 h, 10 mmol of racemic malathion containing 40 mL of sodium phosphate buffer at pH 7.2. Enzyme concentration was 10 % of the substrate mass, conversion, c, enantiomeric excess, ee _p,of desire product (R)-malathion and enantioselectivity, E

ISSN: 2661-801X