Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters
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 t...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Japan Society for Bioscience, Biotechnology, and Agrochemistry
2011
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| Online Access: | http://psasir.upm.edu.my/id/eprint/22357/ http://psasir.upm.edu.my/id/eprint/22357/1/Kinetic%20behaviour%20of%20free%20lipase%20and%20mica.pdf |
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| author | Zaidan, Uswatun Hasanah Abdul Rahman, Mohd Basyaruddin Othman, Siti Salhah Basri, Mahiran Abd. Malek, Emilia Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar |
| author_facet | Zaidan, Uswatun Hasanah Abdul Rahman, Mohd Basyaruddin Othman, Siti Salhah Basri, Mahiran Abd. Malek, Emilia Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar |
| author_sort | Zaidan, Uswatun Hasanah |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T08:31:19Z |
| format | Article |
| id | upm-22357 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T08:31:19Z |
| publishDate | 2011 |
| publisher | Japan Society for Bioscience, Biotechnology, and Agrochemistry |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-223572016-09-26T05:40:40Z http://psasir.upm.edu.my/id/eprint/22357/ Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters Zaidan, Uswatun Hasanah Abdul Rahman, Mohd Basyaruddin Othman, Siti Salhah Basri, Mahiran Abd. Malek, Emilia Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar 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. Japan Society for Bioscience, Biotechnology, and Agrochemistry 2011 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22357/1/Kinetic%20behaviour%20of%20free%20lipase%20and%20mica.pdf 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 http://www.tandfonline.com/doi/abs/10.1271/bbb.110117 10.1271/bbb.110117 |
| spellingShingle | Zaidan, Uswatun Hasanah Abdul Rahman, Mohd Basyaruddin Othman, Siti Salhah Basri, Mahiran Abd. Malek, Emilia Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| title | Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| title_full | Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| title_fullStr | Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| title_full_unstemmed | Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| title_short | Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| title_sort | kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters |
| url | http://psasir.upm.edu.my/id/eprint/22357/ http://psasir.upm.edu.my/id/eprint/22357/ http://psasir.upm.edu.my/id/eprint/22357/ http://psasir.upm.edu.my/id/eprint/22357/1/Kinetic%20behaviour%20of%20free%20lipase%20and%20mica.pdf |