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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...

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Main Authors: Zaidan, Uswatun Hasanah, Abdul Rahman, Mohd Basyaruddin, Othman, Siti Salhah, Basri, Mahiran, Abd. Malek, Emilia, Raja Abdul Rahman, Raja Noor Zaliha, Salleh, Abu Bakar
Format: Article
Language:English
Published: Japan Society for Bioscience, Biotechnology, and Agrochemistry 2011
Online Access:http://psasir.upm.edu.my/id/eprint/22357/1/Kinetic%20behaviour%20of%20free%20lipase%20and%20mica.pdf
http://psasir.upm.edu.my/id/eprint/22357/
http://www.tandfonline.com/doi/abs/10.1271/bbb.110117
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spelling my.upm.eprints.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
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
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.
format Article
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
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
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
title 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_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_sort kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters
publisher Japan Society for Bioscience, Biotechnology, and Agrochemistry
publishDate 2011
url http://psasir.upm.edu.my/id/eprint/22357/1/Kinetic%20behaviour%20of%20free%20lipase%20and%20mica.pdf
http://psasir.upm.edu.my/id/eprint/22357/
http://www.tandfonline.com/doi/abs/10.1271/bbb.110117
_version_ 1643827804431712256
score 13.211869

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