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Catalysts
Special Issues
Hydrolases in Genomic Era: Mining, Structure and Function
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Hydrolases in Genomic Era: Mining, Structure and Function

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (28 February 2022) | Viewed by 9492

Special Issue Editors

Prof. Dr. Kian Mau Goh

E-Mail Website
Guest Editor
Department of Biosciences, Faculty of Science, Universiti Teknologi Malaysia (UTM), Skudai 81300, Johor Bahru, Malaysia
Interests: biodiversity; genetic resources and conservation; enzymology; protein engineering; protein structure; genome; metagenome; rare bacteria; transcriptome; biotechnology; molecular biology
Prof. Dr. Rajesh Kumar Sani

E-Mail Website
Guest Editor
Departments of Chemical and Biological Engineering & Applied Biological Sciences, South Dakota School of Mines and Technology, Rapid City, SD 57701, USA
Interests: rules of life in biofilms grown on 2D materials; extremophilic bioprocessing of solid wastes to biofuels and value-added products; space biology (effects of mg on extremophiles); biogas to liquid fuels (BioGTL, genome editing); biocatalysis (protein engineering and bioinformatics); biomaterials/biopolymers (EPSs and PHAs: biomedical applications)
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Ng Chyan Leong

E-Mail Website
Guest Editor
Institute of Systems Biology. Universiti Kebangsaan Malaysia. 43600 UKM Bangi, Malaysia
Interests: structural biology; biochemistry; molecular biology; functional studies of hypothetical proteins

Special Issue Information

Dear Colleagues, 

For the Special Issue “Hydrolases in Genomic Era: Mining, structure and function”, we are inviting submissions of research articles and reviews in the following areas:

  • Enzymology studies of new or uncommon hydrolases classified in EC 3.x.x.x
  • Hydrolases from extremophiles
  • Omics for novel hydrolase mining, including extensive bioinformatic analyses
  • Structural studies of hydrolase protein
  • Functional studies on domain, motif, conserved region, and catalytic and non-catalytic residues of hydrolases
  • Improvement of hydrolase performance by structurally guided or rationally designed protein engineering
  • Applications of hydrolase

Prof. Dr. Kian Mau Goh
Prof. Dr. Rajesh Kumar Sani
Prof. Dr. Ng Chyan Leong
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • esterase
  • glycosidase
  • amylase
  • cellulase
  • hemicellulase
  • etherase
  • peptidase
  • lipase
  • phosphatase
  • dehalogenase
  • sulfohydrolase
  • hydrolase
  • nucleotidase

Published Papers (3 papers)

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Research

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18 pages, 3490 KiB  
Article
Immobilization of Mutant Phosphotriesterase on Fuller’s Earth Enhanced the Stability of the Enzyme
by Wahhida Latip, Victor Feizal Knight, Ong Keat Khim, Noor Azilah Mohd Kasim, Wan Md Zin Wan Yunus, Mohd Shukuri Mohamad Ali and Siti Aminah Mohd Noor
Catalysts 2021, 11(8), 983; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11080983 - 17 Aug 2021
Cited by 7 | Viewed by 2123
Abstract
Immobilization is a method for making an enzyme more robust in the environment, especially in terms of its stability and reusability. A mutant phosphotriesterase (YT PTE) isolated from Pseudomonas dimunita has been reported to have high proficiency in hydrolyzing the Sp and [...] Read more.
Immobilization is a method for making an enzyme more robust in the environment, especially in terms of its stability and reusability. A mutant phosphotriesterase (YT PTE) isolated from Pseudomonas dimunita has been reported to have high proficiency in hydrolyzing the Sp and Rp-enantiomers of organophosphate chromophoric analogs and therefore has great potential as a decontamination agent and biosensor. This work aims to investigate the feasibility of using Fuller’s earth (FE) as a YT PTE immobilization support and characterize its biochemical features after immobilization. The immobilized YT PTE was found to show improvement in thermal stability with a half-life of 24 h compared to that of the free enzyme, which was only 8 h. The stability of the immobilized YT PTE allowed storage for up to 4 months and reuse for up to 6 times. The immobilized YT PTE showed high tolerance against all tested metal ions, Tween 40 and 80 surfactants and inorganic solvents. These findings showed that the immobilized YT PTE became more robust for use especially with regards to its stability and reusability. These features would enhance the future applicability of this enzyme as a decontamination agent and its use in other suitable industrial applications. Full article
(This article belongs to the Special Issue Hydrolases in Genomic Era: Mining, Structure and Function)
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Review

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25 pages, 3275 KiB  
Review
A Bibliometric Analysis and Review of Pullulan-Degrading Enzymes—Past and Current Trends
by Ummirul Mukminin Kahar, Nurriza Ab Latif, Syazwani Itri Amran, Kok Jun Liew and Kian Mau Goh
Catalysts 2022, 12(2), 143; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12020143 - 24 Jan 2022
Cited by 9 | Viewed by 3669
Abstract
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 α-1,6 glucosidic bonds (and α-1,4 for certain enzyme groups) of [...] Read more.
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 α-1,6 glucosidic bonds (and α-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. Full article
(This article belongs to the Special Issue Hydrolases in Genomic Era: Mining, Structure and Function)
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14 pages, 1698 KiB  
Review
Structure-Function and Industrial Relevance of Bacterial Aminopeptidase P
by Muhamad Nadzmi Omar, Raja Noor Zaliha Raja Abd Rahman, Noor Dina Muhd Noor, Wahhida Latip, Victor Feizal Knight and Mohd Shukuri Mohamad Ali
Catalysts 2021, 11(10), 1157; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11101157 - 26 Sep 2021
Cited by 4 | Viewed by 2846
Abstract
Aminopeptidase P (APPro, E.C 3.4.11.9) cleaves N-terminal amino acids from peptides and proteins where the penultimate residue is proline. This metal-ion-dependent enzyme shares a similar fold, catalytic mechanism, and substrate specificity with methionine aminopeptidase and prolidase. It adopts a canonical pita bread fold [...] Read more.
Aminopeptidase P (APPro, E.C 3.4.11.9) cleaves N-terminal amino acids from peptides and proteins where the penultimate residue is proline. This metal-ion-dependent enzyme shares a similar fold, catalytic mechanism, and substrate specificity with methionine aminopeptidase and prolidase. It adopts a canonical pita bread fold that serves as a structural basis for the metal-dependent catalysis and assembles as a tetramer in crystals. Similar to other metalloaminopeptidase, APPro requires metal ions for its maximal enzymatic activity, with manganese being the most preferred cation. Microbial aminopeptidase possesses unique characteristics compared with aminopeptidase from other sources, making it a great industrial enzyme for various applications. This review provides a summary of recent progress in the study of the structure and function of aminopeptidase P and describes its various applications in different industries as well as its significance in the environment. Full article
(This article belongs to the Special Issue Hydrolases in Genomic Era: Mining, Structure and Function)
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