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Thermostable enzyme research advances: a bibliometric analysis

Thermostable enzymes are enzymes that can withstand elevated temperatures as high as 50 °C without altering their structure or distinctive features. The potential of thermostable enzymes to increase the conversion rate at high temperature has been identified as a key factor in enhancing the efficien...

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Detalles Bibliográficos
Autores principales: Che Hussian, Che Haznie Ayu, Leong, Wai Yie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10043094/
https://www.ncbi.nlm.nih.gov/pubmed/36971917
http://dx.doi.org/10.1186/s43141-023-00494-w
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author Che Hussian, Che Haznie Ayu
Leong, Wai Yie
author_facet Che Hussian, Che Haznie Ayu
Leong, Wai Yie
author_sort Che Hussian, Che Haznie Ayu
collection PubMed
description Thermostable enzymes are enzymes that can withstand elevated temperatures as high as 50 °C without altering their structure or distinctive features. The potential of thermostable enzymes to increase the conversion rate at high temperature has been identified as a key factor in enhancing the efficiency of industrial operations. Performing procedures at higher temperatures with thermostable enzymes minimises the risk of microbial contamination, which is one of the most significant benefits. In addition, it helps reduce substrate viscosity, improve transfer speeds, and increase solubility during reaction operations. Thermostable enzymes offer enormous industrial potential as biocatalysts, especially cellulase and xylanase, which have garnered considerable amount of interest for biodegradation and biofuel applications. As the usage of enzymes becomes more common, a range of performance-enhancing applications are being explored. This article offers a bibliometric evaluation of thermostable enzymes. Scopus databases were searched for scientific articles. The findings indicated that thermostable enzymes are widely employed in biodegradation as well as in biofuel and biomass production. Japan, the United States, China, and India, as along with the institutions affiliated with these nations, stand out as the academically most productive in the field of thermostable enzymes. This study’s analysis exposed a vast number of published papers that demonstrate the industrial potential of thermostable enzymes. These results highlight the significance of thermostable enzyme research for a variety of applications.
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spelling pubmed-100430942023-03-29 Thermostable enzyme research advances: a bibliometric analysis Che Hussian, Che Haznie Ayu Leong, Wai Yie J Genet Eng Biotechnol Review Thermostable enzymes are enzymes that can withstand elevated temperatures as high as 50 °C without altering their structure or distinctive features. The potential of thermostable enzymes to increase the conversion rate at high temperature has been identified as a key factor in enhancing the efficiency of industrial operations. Performing procedures at higher temperatures with thermostable enzymes minimises the risk of microbial contamination, which is one of the most significant benefits. In addition, it helps reduce substrate viscosity, improve transfer speeds, and increase solubility during reaction operations. Thermostable enzymes offer enormous industrial potential as biocatalysts, especially cellulase and xylanase, which have garnered considerable amount of interest for biodegradation and biofuel applications. As the usage of enzymes becomes more common, a range of performance-enhancing applications are being explored. This article offers a bibliometric evaluation of thermostable enzymes. Scopus databases were searched for scientific articles. The findings indicated that thermostable enzymes are widely employed in biodegradation as well as in biofuel and biomass production. Japan, the United States, China, and India, as along with the institutions affiliated with these nations, stand out as the academically most productive in the field of thermostable enzymes. This study’s analysis exposed a vast number of published papers that demonstrate the industrial potential of thermostable enzymes. These results highlight the significance of thermostable enzyme research for a variety of applications. Springer Berlin Heidelberg 2023-03-27 /pmc/articles/PMC10043094/ /pubmed/36971917 http://dx.doi.org/10.1186/s43141-023-00494-w Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Review
Che Hussian, Che Haznie Ayu
Leong, Wai Yie
Thermostable enzyme research advances: a bibliometric analysis
title Thermostable enzyme research advances: a bibliometric analysis
title_full Thermostable enzyme research advances: a bibliometric analysis
title_fullStr Thermostable enzyme research advances: a bibliometric analysis
title_full_unstemmed Thermostable enzyme research advances: a bibliometric analysis
title_short Thermostable enzyme research advances: a bibliometric analysis
title_sort thermostable enzyme research advances: a bibliometric analysis
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10043094/
https://www.ncbi.nlm.nih.gov/pubmed/36971917
http://dx.doi.org/10.1186/s43141-023-00494-w
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