Biocatalytic production of lactose ester catalysed by mica-based immobilised lipase

• Main Authors: Uswatun Hasanah, Zaidan,, Mohd Basyaruddin Abdul, Rahman,, Mahiran, Basri,, Emilia, Abdulmalek,, Siti Salhah, Othman,, Raja Noor Zaliha Raja, Abdul Rahman,, Abu Bakar, Salleh,
• Format: Article
• Language: English
• Published: Elsevier Sci Ltd 2015
• Subjects: Mica; Candida Rugosa Lipase; Covalent Bonding; Cross-Linking; Sugar Esters
• Online Access: http://ddms.usim.edu.my/handle/123456789/8078; http://ac.els-cdn.com/S030881461101209X/1-s2.0-S030881461101209X-main.pdf?_tid=cefbf148-aea6-11e5-9633-00000aacb35d&acdnat=1451446896_af8ea5f7ce3e8e6dff45f831708f551d

Enzyme immobilisation technology is an effective means to improve sugar ester production through the employment of biocatalysts. In the present study, immobilisation of Candida rugosa (CRL) lipase onto amino-activated mica is performed via covalent bonding (namely Amino-CRL) and the cross-linking of lipases into nano-reactors through physical adsorption (namely NER-CRL). Free and immobilised lipases were tested for their esterification activities. Specific activities for Amino-CRL and NER-CRL increased by 2.4 and 2.6-fold, respectively, upon immobilisation. Extending this work, immobilised lipases have novel capabilities in the synthesis of sugar esters. The optimised conditions for sugar fatty acid ester syntheses are 48 h at 2:1 of molar ratio of lactose sugar to capric acid at 55 C. Furthermore, a high operational stability with half-lives of over 13 and 10 runs was achieved for NER-CRL and Amino-CRL, respectively, indicating the efficiency of the immobilisation process. (C) 2011 Elsevier Ltd. All rights reserved.