Zaidan U.H.Rahman M.B.A.Othman S.S.Basri M.Abdulmalek E.Rahman R.N.Z.R.A.Salleh A.B.2024-05-292024-05-292011916845110.1271/bbb.1101172-s2.0-80052020034https://www.scopus.com/inward/record.uri?eid=2-s2.0-80052020034&doi=10.1271%2fbbb.110117&partnerID=40&md5=7ea0ac83f2963ae42fc517c48ccd5cb6https://oarep.usim.edu.my/handle/123456789/1028921821960The utilization of natural mica as a biocatalyst support in kinetic investigations is first described in this study. The formation of lactose caprate from lactose sugar and capric acid, using free lipase (free-CRL) and lipase immobilized on nanoporous mica (NER-CRL) as a biocatalyst, was evaluated through a kinetic study. The apparent kinetic parameters, Km and Vmax, were determined by means of the Michaelis-Menten kinetic model. The Ping-Pong Bi-Bi mechanism with single substrate inhibition was adopted as it best explains the experimental findings. The kinetic results show lower Km values with NER-CRL than with free-CRL, indicating the higher affinity of NER-CRL towards both substrates at the maximum reaction velocity (Vmax,app > Vmax). The kinetic parameters deduced from this model were used to simulate reaction rate data which were in close agreement with the experimental values.en-USKinetic studyLipase immobilizationMicaPing-Pong Bi-Bi modelSugar ester synthesisArticle14461450758BBBIE