Zaidan U.H.Abdul Rahman M.B.Othman S.S.Basri M.Abdulmalek E.Abdul Rahman R.N.Z.R.Salleh A.B.2024-05-292024-05-292012308814610.1016/j.foodchem.2011.08.0602-s2.0-80054024932https://www.scopus.com/inward/record.uri?eid=2-s2.0-80054024932&doi=10.1016%2fj.foodchem.2011.08.060&partnerID=40&md5=74d5086cd6c9f9fe0644e23bd97d49e3https://oarep.usim.edu.my/handle/123456789/10083Enzyme 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. � 2011 Elsevier Ltd. All rights reserved.en-USCandida rugosa lipaseCovalent bondingCross-linkingMicaSugar estersArticle1992051311FOCHD