Kinetic study of soybean pure powder lecithin hydrolysis using immobilized phospholipase A2

Grasas y Aceites

N. Zaritzky¹  C. Camusso²  B. Maroto² 

[1] Depto de Ingeniería Química. Facultad de Ingeniería UNLP y CIDCA. Facultad de Ciencias Exactas, Universidad Nacional de La Plata;Facultad de Ciencias Agropecuarias, Universidad Nacional de Córdoba;

关键词: a₂ phospholipase enzyme;    enzymatic hydrolysis;    immobilized enzymes;    soybean lecithin;   

DOI  :  10.3989/gya.2001.v52.i1.393

来源: DOAJ

【 摘 要 】

Immobilized A2 phospholipase enzyme promotes the hydrolytic reaction of pure powder soybean lecithin releasing a mole of fatty acid from C-2 position. The main purpose of this paper was to determine the kinetic parameters of this reaction when the enzyme was adsorbed on alumina or DEAE-sephadex. The best conditions for the reaction were: temperature: 45-48ºC, Ca ions concentration: 6mM, pH: 8,65. Tested conditions for substrate concentration were: 6,3; 12,7; 19 and 25 mM working in a batch type reactor and with the immobilized enzyme. The incubating time did not change the enzymatic activity. The hydrolytic activity of alumina or DEAE-sephadex adsorbed A2 phospholipase enzyme was lower than of the soluble enzyme because the intrinsic properties are modified by immobilization. For substrate concentrations ranging between 6 and 19 mM first order kinetic velocity constants were k = 9, 88. 10-2 min-1 and k = 1,766. 10-1 min-1 for alumina and DEAEsephadex respectively. For the same supports but at higher substrate concentration (25mM) the zero order kinetic velocity constants were k= 1,62. 10-3 mol.l-1min-1 (alumina) and k = 3,58. 10-3 mol.l-1 min-1 (DEAE-sephadex).

【 授权许可】

Unknown