A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends

Starch and pullulan degrading enzymes are essential industrial biocatalysts. Pullulan-degrading enzymes are grouped into pullulanases (types I and type II) and pullulan hydrolase (types I, II and III). Generally, these enzymes hydrolyse the a-1,6 glucosidic bonds (and a-1,4 for certain enzyme groups...

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主要な著者: Kahar, Ummirul Mukminin, Ab. Latif, Nurriza, Amran, Syazwani Itri, Liew, Kok Jun, Goh, Kian Mau
フォーマット: 論文
言語:English
出版事項: MDPI 2022
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オンライン・アクセス:http://eprints.utm.my/id/eprint/101322/1/GohKianMau2022_ABibliometricAnalysisandReviewofPullulanDegrading.pdf
http://eprints.utm.my/id/eprint/101322/
http://dx.doi.org/10.3390/catal12020143
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spelling my.utm.1013222023-06-08T09:01:26Z http://eprints.utm.my/id/eprint/101322/ A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends Kahar, Ummirul Mukminin Ab. Latif, Nurriza Amran, Syazwani Itri Liew, Kok Jun Goh, Kian Mau QD Chemistry Starch and pullulan degrading enzymes are essential industrial biocatalysts. Pullulan-degrading enzymes are grouped into pullulanases (types I and type II) and pullulan hydrolase (types I, II and III). Generally, these enzymes hydrolyse the a-1,6 glucosidic bonds (and a-1,4 for certain enzyme groups) of substrates and form reducing sugars such as glucose, maltose, maltotriose, panose or isopanose. This review covers two main aspects: (i) bibliometric analysis of publications and patents related to pullulan-degrading enzymes and (ii) biological aspects of free and immobilised pullulan-degrading enzymes and protein engineering. The collective data suggest that most publications involved researchers within the same institution or country in the past and current practice. Multi-national interaction shall be improved, especially in tapping the enzymes from unculturable prokaryotes. While the understanding of pullulanases may reach a certain extend of saturation, the discovery of pullulan hydrolases is still limited. In this report, we suggest readers consider using the next-generation sequencing technique to fill the gaps of finding more new sequences encoding pullulan-degrading enzymes to expand the knowledge body of this topic. MDPI 2022 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/101322/1/GohKianMau2022_ABibliometricAnalysisandReviewofPullulanDegrading.pdf Kahar, Ummirul Mukminin and Ab. Latif, Nurriza and Amran, Syazwani Itri and Liew, Kok Jun and Goh, Kian Mau (2022) A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends. Catalysts, 12 (2). pp. 1-25. ISSN 2073-4344 http://dx.doi.org/10.3390/catal12020143 DOI : 10.3390/catal12020143
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic QD Chemistry
spellingShingle QD Chemistry
Kahar, Ummirul Mukminin
Ab. Latif, Nurriza
Amran, Syazwani Itri
Liew, Kok Jun
Goh, Kian Mau
A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends
description Starch and pullulan degrading enzymes are essential industrial biocatalysts. Pullulan-degrading enzymes are grouped into pullulanases (types I and type II) and pullulan hydrolase (types I, II and III). Generally, these enzymes hydrolyse the a-1,6 glucosidic bonds (and a-1,4 for certain enzyme groups) of substrates and form reducing sugars such as glucose, maltose, maltotriose, panose or isopanose. This review covers two main aspects: (i) bibliometric analysis of publications and patents related to pullulan-degrading enzymes and (ii) biological aspects of free and immobilised pullulan-degrading enzymes and protein engineering. The collective data suggest that most publications involved researchers within the same institution or country in the past and current practice. Multi-national interaction shall be improved, especially in tapping the enzymes from unculturable prokaryotes. While the understanding of pullulanases may reach a certain extend of saturation, the discovery of pullulan hydrolases is still limited. In this report, we suggest readers consider using the next-generation sequencing technique to fill the gaps of finding more new sequences encoding pullulan-degrading enzymes to expand the knowledge body of this topic.
format Article
author Kahar, Ummirul Mukminin
Ab. Latif, Nurriza
Amran, Syazwani Itri
Liew, Kok Jun
Goh, Kian Mau
author_facet Kahar, Ummirul Mukminin
Ab. Latif, Nurriza
Amran, Syazwani Itri
Liew, Kok Jun
Goh, Kian Mau
author_sort Kahar, Ummirul Mukminin
title A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends
title_short A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends
title_full A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends
title_fullStr A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends
title_full_unstemmed A bibliometric analysis and review of Pullulan-Degrading enzymes—Past and current trends
title_sort bibliometric analysis and review of pullulan-degrading enzymes—past and current trends
publisher MDPI
publishDate 2022
url http://eprints.utm.my/id/eprint/101322/1/GohKianMau2022_ABibliometricAnalysisandReviewofPullulanDegrading.pdf
http://eprints.utm.my/id/eprint/101322/
http://dx.doi.org/10.3390/catal12020143
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