Synthesis of Retinyl Palmitate Catalyzed by Candida sp. 99-125 Lipase Immobilized on Fiber-Like SBA-15 Mesoporous Material

Authors: Kai, Zhu; Jianqiang, Wang; Yan-Hua, Wang; Hui, Liu; Ping-Fang, Han; Ping, Wei

Source: Journal of Nanoscience and Nanotechnology, Volume 11, Number 9, September 2011 , pp. 7593-7602(10)

Publisher: American Scientific Publishers

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Abstract:

Candida sp. 99-125 lipase was suitable for transesterification of fats and oils to produce fatty acid methyl ester. The adsorption of Candida sp. 99-125 lipase onto the fiber-like SBA-15 mesoporous material has been studied. The unaltered structural order of the fiber-like SBA-15 before and after the adsorption has been confirmed by FT-IR, SEM and N2 adsorption. The amount of adsorbed Candida sp. 99-125 lipase depends both on the solution pH and reaction time. Good adsorption capacity of Candida sp. 99-125 lipase on fiber-like SBA-15 may be due to solution pH from 5.0 to 9.0 especially at 7.0 (93.99 mg enzyme per gram silica is obtained and the activity recovery is 281.05%). A high lipase loading (135.9 mg enzyme per gram silica) was obtained, but it did not produce a proportionate level of catalytic activity. The immobilized Candida sp. 99-125 lipase showed increased adaptability in the hydrolysis of p-nitrophenyl acetate compared to free Candida sp. 99-125 lipase at pH 5.0–9.0. Meanwhile, the immobilized Candida sp. 99-125 lipase showed higher thermal stability than that of free Candida sp. 99-125 lipase. And the synthesis of retinyl palmitate in organic solvent with the immobilized Candida sp. 99-125 lipase was investigated. The influence factors, such as: the solvent used, the molar ratio and concentrations of substrates, the reaction time and the amount of lipase were studied and optimized. In the conditions of transesterificating 0.164 g retinyl acetate and 0.32 g palmitic acid, 10 mL of solvent hexane, 1:4 of mass ratio of lipase to retinyl acetate, and 6 hours of reaction time, 74.6% of retinyl acetate was converted into retinyl plamitate.

Keywords: CANDIDA SP. 99-125 LIPASE; HYDROLYSIS ACTIVITY; IMMOBILIZATION; SBA-15

Document Type: Research Article

DOI: http://dx.doi.org/10.1166/jnn.2011.4731

Publication date: September 1, 2011

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  • Journal for Nanoscience and Nanotechnology (JNN) is an international and multidisciplinary peer-reviewed journal with a wide-ranging coverage, consolidating research activities in all areas of nanoscience and nanotechnology into a single and unique reference source. JNN is the first cross-disciplinary journal to publish original full research articles, rapid communications of important new scientific and technological findings, timely state-of-the-art reviews with author's photo and short biography, and current research news encompassing the fundamental and applied research in all disciplines of science, engineering and medicine.
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