Structural effects of amphiphiles on Candida rugosa lipase activation by freeze-drying of aqueous solution of enzyme and amphiphile

• Published in: Journal of Bioscience and Bioengineering Vol. 96; no. 6; pp. 525 - 528
• Main Authors: Mine, Yurie, Fukunaga, Kimitoshi, Samejima, Ken-Ichi, Yoshimoto, Makoto, Nakao, Katsumi, Sugimura, Yoshiaki
• Format: Book Review Journal Article
• Language: English
• Published: Amsterdarm Elsevier B.V 2003; Elsevier Science
• Subjects: amphiphile; amphiphiles; Biological and medical sciences; Biotechnology; CANDIDA RUGOSA; Candida rugosa lipase; FREEZE DRYING; Fundamental and applied biological sciences. Psychology; modified lipase; nonaqueous enzymology; SURFACTANTS; TRIACYLGLYCEROL LIPASE; modified lipase; nonaqueous enzymology; Candida rugosa lipase; amphiphile; Freeze drying; Enzyme; Triacylglycerol lipase; Esterases; Activation; Amphiphilic compound; Carboxylic ester hydrolases; Fungi; Hydrolases; Fungi Imperfecti; Aqueous solution; Candida rugosa; Thallophyta
• ISSN: 1389-1723; 1347-4421
• DOI: 10.1016/S1389-1723(04)70144-9

Lipases co-lyophilized with water-soluble gemini-type amphiphiles were found to have high enzyme activity in nonaqueous media without washing out of the amphiphile with anhydrous organic solvent. In this study, we obtained freeze-dried complexes of Candida rugosa lipase (CRL) with six water-soluble twin glusitol-headed amphiphiles bearing different types of hydrophobic tails, including newly synthesized ones, and their transesterification activity in organic solvent was evaluated. The results indicate that the increased enzyme activity upon CRL modification at 200 molar ratio of amphiphile/CRL, which are restricted to the ester-containing amphiphiles, is probably due to the surface activation by the interaction between ester-carbonyl of the amphiphile and phenyl group of the tyrosine residue situated on the surface of the lid in the CRL.