title: Studies of optimum conditions for covalent immobilization of Candida rugosa lipase on poly(gamma-glutamic acid) by RSM.
abstract: Poly(gamma-glutamic acid) (gamma-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on gamma-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2-6h), immobilization temperature (0-26 degrees C), and enzyme/support ratio (0.1-0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3h, immobilization temperature 13.3 degrees C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
authors: Department of Nutrition and Health Science, Chung-Chou University of Technology, No.6, Lane 2, Sec.3, Shanjiao Rd. Yuan-Lin, Chang-Hua 503, Taiwan.
authors: S-W
authors: SW
authors: Chang
authors: J-F
authors: JF
authors: Shaw
authors: K-H
authors: KH
authors: Yang
authors: S-F
authors: SF
authors: Chang
authors: C-J
authors: CJ
authors: Shieh
mesh_terms: D002175:Candida / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D011099:Polyglutamic Acid; D013816:Thermodynamics; D014280:Triglycerides / Q000378:metabolism
chemical_list: D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D014280:Triglycerides; D011099:Polyglutamic Acid; D008049:Lipase