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Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters


Zaidan, Uswatun Hasanah and Abdul Rahman, Mohd Basyaruddin and Othman, Siti Salhah and Basri, Mahiran and Abd. Malek, Emilia and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar (2011) Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters. Bioscience, Biotechnology, and Biochemistry, 75 (8). pp. 1446-1450. ISSN 0916-8451; ESSN: 1347-6947


The 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, K(m) and V(max), 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 K(m) values with NER-CRL than with free-CRL, indicating the higher affinity of NER-CRL towards both substrates at the maximum reaction velocity (V(max,app)>V(max)). The kinetic parameters deduced from this model were used to simulate reaction rate data which were in close agreement with the experimental values.

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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Faculty of Science
DOI Number: https://doi.org/10.1271/bbb.110117
Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Keywords: Lipase immobilization; Mica; Kinetic study; Ping-Pong Bi-Bi model; Sugar ester synthesis
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 01 Sep 2015 04:59
Last Modified: 26 Sep 2016 05:40
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1271/bbb.110117
URI: http://psasir.upm.edu.my/id/eprint/22357
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