Thermostable lipases and their dynamics of improved enzymatic properties

Thermal stability is one of the most desirable characteristics in the search for novel lipases. The search for thermophilic microorganisms for synthesising functional enzyme biocatalysts with the ability to withstand high temperature, and capacity to maintain their native state in extreme conditions...

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Main Authors: Hamdan, Siti Hajar, Maiangwa, Jonathan, Mohamad Ali, Mohd Shukuri, M. Normi, Yahaya, Sabri, Suriana, Leow, Thean Chor
Format: Article
Language:English
Published: Springer 2021
Online Access:http://psasir.upm.edu.my/id/eprint/95610/1/Thermostable%20lipases%20and%20their%20dynamics%20of%20improved%20enzymatic%20properties.pdf
http://psasir.upm.edu.my/id/eprint/95610/
https://link.springer.com/article/10.1007/s00253-021-11520-7
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spelling my.upm.eprints.956102022-07-13T05:40:34Z http://psasir.upm.edu.my/id/eprint/95610/ Thermostable lipases and their dynamics of improved enzymatic properties Hamdan, Siti Hajar Maiangwa, Jonathan Mohamad Ali, Mohd Shukuri M. Normi, Yahaya Sabri, Suriana Leow, Thean Chor Thermal stability is one of the most desirable characteristics in the search for novel lipases. The search for thermophilic microorganisms for synthesising functional enzyme biocatalysts with the ability to withstand high temperature, and capacity to maintain their native state in extreme conditions opens up new opportunities for their biotechnological applications. Thermophilic organisms are one of the most favoured organisms, whose distinctive characteristics are extremely related to their cellular constituent particularly biologically active proteins. Modifications on the enzyme structure are critical in optimizing the stability of enzyme to thermophilic conditions. Thermostable lipases are one of the most favourable enzymes used in food industries, pharmaceutical field, and actively been studied as potential biocatalyst in biodiesel production and other biotechnology application. Particularly, there is a trade-off between the use of enzymes in high concentration of organic solvents and product generation. Enhancement of the enzyme stability needs to be achieved for them to maintain their enzymatic activity regardless the environment. Various approaches on protein modification applied since decades ago conveyed a better understanding on how to improve the enzymatic properties in thermophilic bacteria. In fact, preliminary approach using advanced computational analysis is practically conducted before any modification is being performed experimentally. Apart from that, isolation of novel extremozymes from various microorganisms are offering great frontier in explaining the crucial native interaction within the molecules which could help in protein engineering. In this review, the thermostability prospect of lipases and the utility of protein engineering insights into achieving functional industrial usefulness at their high temperature habitat are highlighted. Similarly, the underlying thermodynamic and structural basis that defines the forces that stabilize these thermostable lipase is discussed. Springer 2021 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/95610/1/Thermostable%20lipases%20and%20their%20dynamics%20of%20improved%20enzymatic%20properties.pdf Hamdan, Siti Hajar and Maiangwa, Jonathan and Mohamad Ali, Mohd Shukuri and M. Normi, Yahaya and Sabri, Suriana and Leow, Thean Chor (2021) Thermostable lipases and their dynamics of improved enzymatic properties. Applied Microbiology and Biotechnology, 105. 7069 - 7094. ISSN 0175-7598; ESSN: 1432-0614 https://link.springer.com/article/10.1007/s00253-021-11520-7 10.1007/s00253-021-11520-7
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 Thermal stability is one of the most desirable characteristics in the search for novel lipases. The search for thermophilic microorganisms for synthesising functional enzyme biocatalysts with the ability to withstand high temperature, and capacity to maintain their native state in extreme conditions opens up new opportunities for their biotechnological applications. Thermophilic organisms are one of the most favoured organisms, whose distinctive characteristics are extremely related to their cellular constituent particularly biologically active proteins. Modifications on the enzyme structure are critical in optimizing the stability of enzyme to thermophilic conditions. Thermostable lipases are one of the most favourable enzymes used in food industries, pharmaceutical field, and actively been studied as potential biocatalyst in biodiesel production and other biotechnology application. Particularly, there is a trade-off between the use of enzymes in high concentration of organic solvents and product generation. Enhancement of the enzyme stability needs to be achieved for them to maintain their enzymatic activity regardless the environment. Various approaches on protein modification applied since decades ago conveyed a better understanding on how to improve the enzymatic properties in thermophilic bacteria. In fact, preliminary approach using advanced computational analysis is practically conducted before any modification is being performed experimentally. Apart from that, isolation of novel extremozymes from various microorganisms are offering great frontier in explaining the crucial native interaction within the molecules which could help in protein engineering. In this review, the thermostability prospect of lipases and the utility of protein engineering insights into achieving functional industrial usefulness at their high temperature habitat are highlighted. Similarly, the underlying thermodynamic and structural basis that defines the forces that stabilize these thermostable lipase is discussed.
format Article
author Hamdan, Siti Hajar
Maiangwa, Jonathan
Mohamad Ali, Mohd Shukuri
M. Normi, Yahaya
Sabri, Suriana
Leow, Thean Chor
spellingShingle Hamdan, Siti Hajar
Maiangwa, Jonathan
Mohamad Ali, Mohd Shukuri
M. Normi, Yahaya
Sabri, Suriana
Leow, Thean Chor
Thermostable lipases and their dynamics of improved enzymatic properties
author_facet Hamdan, Siti Hajar
Maiangwa, Jonathan
Mohamad Ali, Mohd Shukuri
M. Normi, Yahaya
Sabri, Suriana
Leow, Thean Chor
author_sort Hamdan, Siti Hajar
title Thermostable lipases and their dynamics of improved enzymatic properties
title_short Thermostable lipases and their dynamics of improved enzymatic properties
title_full Thermostable lipases and their dynamics of improved enzymatic properties
title_fullStr Thermostable lipases and their dynamics of improved enzymatic properties
title_full_unstemmed Thermostable lipases and their dynamics of improved enzymatic properties
title_sort thermostable lipases and their dynamics of improved enzymatic properties
publisher Springer
publishDate 2021
url http://psasir.upm.edu.my/id/eprint/95610/1/Thermostable%20lipases%20and%20their%20dynamics%20of%20improved%20enzymatic%20properties.pdf
http://psasir.upm.edu.my/id/eprint/95610/
https://link.springer.com/article/10.1007/s00253-021-11520-7
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