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Applied Sciences
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Carbohydrate-Active Enzymes for Valuable Product Creation
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Carbohydrate-Active Enzymes for Valuable Product Creation

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Applied Biosciences and Bioengineering".

Deadline for manuscript submissions: closed (31 October 2021) | Viewed by 4480

Special Issue Editor

Dr. Birgitte Zeuner

E-Mail Website
Guest Editor
Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark
Interests: enzyme technology; enzymatic transglycosylation; enzymatic oligosaccharide synthesis; protein engineering; protein structure and structure–function relationships; bioinformatics; analysis of carbohydrates and plant cell wall phenolics; bioactive oligosaccharides; prebiotics; human milk oligosaccharides; enzyme kinetics; assay design; bioprocess technology; tailored pectin degradation; enzyme immobilization

Special Issue Information

Dear Colleagues,

I hereby invite you to contribute to a Special Issue in the journal Applied Sciences on the topic of “Carbohydrate-Active Enzymes for Valuable Product Creation”.

This Special Issue will cover recent developments in the field of carbohydrate-active enzyme technology, focusing on solutions to create valuable compounds. Examples include, but are not limited to, prebiotics or similarly bioactive compounds as well as on enzymatic treatment of biocommodities to increase their value and/or expand their range of application. Examples of biocommodity engineering include enzymatic depolymerization or extraction of defined carbohydrate structures, for example to increase the product value or improve product properties compared to the starting material. The scope also covers enzymatic technologies to synthesize carbohydrates, for example transglycosylation or use of glycosyltransferases. This Special Issue aims to include examples of more than one of these strategies and welcomes research that compares different routes to production of defined carbohydrates. Recent developments in the field include diverse research areas, such as enzyme discovery, protein engineering, computational modelling methods, carbohydrate analysis, development of appropriate enzyme cocktails, and bioprocess engineering.

Thus, I invite you to submit your research on these topics, in the form of original research papers or insightful review articles.

Dr. Birgitte Zeuner
Guest Editor

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. Applied Sciences is an international peer-reviewed open access semimonthly 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 2400 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

  • Prebiotics
  • Bioactive carbohydrates
  • Enzymatic carbohydrate synthesis
  • Enzymatic glycosynthesis
  • Transglycosylation
  • Tailored carbohydrate degradation
  • Biocommodity engineering
  • Enzymatic extraction
  • Enzymatic depolymerization
  • Bioprocessing
  • Bioprocess engineering
  • Enzyme discovery
  • Protein engineering
  • Carbohydrate-active enzymes

Published Papers (2 papers)

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Research

17 pages, 9181 KiB  
Article
A Comparison of the Transglycosylation Capacity between the Guar GH27 Aga27A and Bacteroides GH36 BoGal36A α-Galactosidases
by Mathias Wiemann, Emil Axell and Henrik Stålbrand
Appl. Sci. 2022, 12(10), 5123; https://0-doi-org.brum.beds.ac.uk/10.3390/app12105123 - 19 May 2022
Cited by 1 | Viewed by 1364
Abstract
The transglycosylation behavior and capacity of two clan GH-D α-galactosidases, BoGal36A from the gut bacterium Bacteroides ovatus and Aga27A from the guar plant, was investigated and compared. The enzymes were screened for the ability to use para-nitrophenyl-α-galactoside (pNP-Gal), raffinose and locust [...] Read more.
The transglycosylation behavior and capacity of two clan GH-D α-galactosidases, BoGal36A from the gut bacterium Bacteroides ovatus and Aga27A from the guar plant, was investigated and compared. The enzymes were screened for the ability to use para-nitrophenyl-α-galactoside (pNP-Gal), raffinose and locust bean gum (LBG) galactomannan as glycosyl donors with the glycosyl acceptors methanol, propanol, allyl alcohol, propargyl alcohol and glycerol using mass spectrometry. Aga27A was, in general, more stable in the presence of the acceptors. HPLC analysis was developed and used as a second screening method for reactions using raffinose or LBG as a donor substrate with methanol, propanol and glycerol as acceptors. Time-resolved reactions were set up with raffinose and methanol as the donor and acceptor, respectively, in order to develop an insight into the basic transglycosylation properties, including the ratio between the rate of transglycosylation (methyl galactoside synthesis) and rate of hydrolysis. BoGal36A had a somewhat higher ratio (0.99 compared to 0.71 for Aga27A) at early time points but was indicated to be more prone to secondary (product) hydrolysis in prolonged incubations. The methyl galactoside yield was higher when using raffinose (48% for BoGal36A and 38% for Aga27A) compared to LBG (27% for BoGal36A and 30% for Aga27A). Full article
(This article belongs to the Special Issue Carbohydrate-Active Enzymes for Valuable Product Creation)
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23 pages, 5152 KiB  
Article
Improvement of the Transglycosylation Efficiency of a Lacto-N-Biosidase from Bifidobacterium bifidum by Protein Engineering
by Marlene Vuillemin, Jesper Holck, Martin Matwiejuk, Eduardo S. Moreno Prieto, Jan Muschiol, Dora Molnar-Gabor, Anne S. Meyer and Birgitte Zeuner
Appl. Sci. 2021, 11(23), 11493; https://0-doi-org.brum.beds.ac.uk/10.3390/app112311493 - 04 Dec 2021
Cited by 7 | Viewed by 2368
Abstract
The lacto-N-biosidase LnbB from Bifidobacterium bifidum JCM 1254 was engineered to improve its negligible transglycosylation efficiency with the purpose of enzymatically synthesizing lacto-N-tetraose (LNT; Gal-β1,3-GlcNAc-β1,3-Gal-β1,4-Glc) in one enzymatic step. LNT is a prebiotic human milk oligosaccharide in itself and [...] Read more.
The lacto-N-biosidase LnbB from Bifidobacterium bifidum JCM 1254 was engineered to improve its negligible transglycosylation efficiency with the purpose of enzymatically synthesizing lacto-N-tetraose (LNT; Gal-β1,3-GlcNAc-β1,3-Gal-β1,4-Glc) in one enzymatic step. LNT is a prebiotic human milk oligosaccharide in itself and constitutes the structural core of a range of more complex human milk oligosaccharides as well. Thirteen different LnbB variants were expressed and screened for transglycosylation activity by monitoring transglycosylation product formation using lacto-N-biose 1,2-oxazoline as donor substrate and lactose as acceptor substrate. LNT was the major reaction product, yet careful reaction analysis revealed the formation of three additional LNT isomers, which we identified to have a β1,2-linkage, a β1,6-linkage, and a 1,1-linkage, respectively, between lacto-N-biose (Gal-β1,3-GlcNAc) and lactose. Considering both maximal transglycosylation yield and regioselectivity as well as minimal product hydrolysis, the best variant was LnbB W394H, closely followed by W465H and Y419N. A high transglycosylation yield was also obtained with W394F, yet the substitution of W394 and W465 of the subsite −1 hydrophobic platform in the enzyme with His dramatically impaired the undesirable product hydrolysis as compared to substitution with Phe; the effect was most pronounced for W465. Using p-nitrophenyl-β-lacto-N-bioside as donor substrate manifested W394 as an important target position. The optimization of the substrate concentrations confirmed that high initial substrate concentration and high acceptor-to-donor ratio both favor transglycosylation. Full article
(This article belongs to the Special Issue Carbohydrate-Active Enzymes for Valuable Product Creation)
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