4.6 Article

A Bibliometric Analysis and Review of Pullulan-Degrading Enzymes-Past and Current Trends

期刊

CATALYSTS
卷 12, 期 2, 页码 -

出版社

MDPI
DOI: 10.3390/catal12020143

关键词

amylopullulanase; alpha-amylase-pullulanase; carbohydrate-active enzyme; glycoside hydrolase; isopullulanase; neopullulanase; pullulan; pullulan hydrolase; starch; type I pullulanase

资金

  1. Malaysia FRGS [FRGS/1/2020/WAB11/MESTECC/02/1]
  2. National Institutes of Biotechnology Malaysia (NIBM) Seed Fund [NIBM/SF/2021-13]
  3. Malaysia Fundamental Research Grant Scheme (FRGS) [5F241, 5F245, FRGS/1/2019/STG03/UTM/02/1, FRGS/1/2019/STG04/UTM/02/4]
  4. [2021 (NIBM/SF/2021-13)]

向作者/读者索取更多资源

This review provides a bibliometric analysis of publications and patents related to pullulan-degrading enzymes, as well as an overview of the biological aspects and protein engineering of these enzymes. The data suggest the need for improved international collaboration and the use of next-generation sequencing techniques to expand the knowledge about pullulan-degrading enzyme sequences.
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 alpha-1,6 glucosidic bonds (and alpha-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.

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