The increased efficiency of porphyran hydrolysis by constructing a multifunctional enzyme complex from marine microorganisms.


Journal

Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761

Informations de publication

Date de publication:
Apr 2023
Historique:
received: 03 11 2022
revised: 23 12 2022
accepted: 24 01 2023
pubmed: 30 1 2023
medline: 7 3 2023
entrez: 29 1 2023
Statut: ppublish

Résumé

Porphyran, a polysaccharide composed of red algae, is a source of a multifunctional oligosaccharide material and raw biomass with various physiological activities. The glycolysis of porphyrans into oligosaccharides through various porphyranases is an approach for obtaining high-quality and promising alternative resources. In this study, porphyran was extracted from Porphyra yezoensis and used as a research substrate. We also established an efficient hydrolysis method using an enzymatic complex obtained through cohesin-dockerin interactions that degrade natural polysaccharides. The cohesion-dockerin interaction is designed to genetically bind the dockerin module to the end of an existing enzyme and then attach the cohesin module to obtain a protein complex. The designed protein complex has been shown to further increase the activity on the substrate, which can be considered a useful method to obtain efficient oligosaccharides or monosaccharides through hydrolysis of red algae for bioresources.

Identifiants

pubmed: 36709516
pii: S0141-0229(23)00015-7
doi: 10.1016/j.enzmictec.2023.110207
pii:
doi:

Substances chimiques

Multifunctional Enzymes 0
porphyran 11016-36-7
Multienzyme Complexes 0
Sepharose 9012-36-6
Bacterial Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

110207

Informations de copyright

Copyright © 2023 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

JooHee Han (J)

Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea; Department of Food Science and Biotechnology, College of Knowledge-Based Services Engineering, Sungshin Women's University, Seoul 01133, Republic of Korea.

YeWon Jo (Y)

Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea; Department of Food Science and Biotechnology, College of Knowledge-Based Services Engineering, Sungshin Women's University, Seoul 01133, Republic of Korea.

Habin Sun (H)

Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea; Department of Food Science and Biotechnology, College of Knowledge-Based Services Engineering, Sungshin Women's University, Seoul 01133, Republic of Korea.

Sung Ok Han (SO)

Department of Biotechnology, Korea University, Seoul 02841, Republic of Korea; Department of Food Science and Biotechnology, College of Knowledge-Based Services Engineering, Sungshin Women's University, Seoul 01133, Republic of Korea.

Jeong Eun Hyeon (JE)

Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea; Department of Biotechnology, Korea University, Seoul 02841, Republic of Korea; Department of Food Science and Biotechnology, College of Knowledge-Based Services Engineering, Sungshin Women's University, Seoul 01133, Republic of Korea. Electronic address: hyeonje@sungshin.ac.kr.

Articles similaires

Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria

Two codependent routes lead to high-level MRSA.

Abimbola Feyisara Adedeji-Olulana, Katarzyna Wacnik, Lucia Lafage et al.
1.00
Methicillin-Resistant Staphylococcus aureus Penicillin-Binding Proteins Peptidoglycan Bacterial Proteins Anti-Bacterial Agents
Mycobacterium tuberculosis Animals Guinea Pigs Bacterial Proteins Toxin-Antitoxin Systems

Helicobacter pylori biofilm interference by N-acyl homoserine lactonases: in vitro and in silico approaches.

Vinoj Gopalakrishnan, Vaijayanthi Saravanan, Maria Infant Majula Shifani Mahendran et al.
1.00
Biofilms Helicobacter pylori Bacterial Proteins Carboxylic Ester Hydrolases Molecular Docking Simulation

Classifications MeSH