Biochemical and molecular characterization of an acido-thermostable endo-chitinase from Bacillus altitudinis KA15 for industrial degradation of chitinous waste.

Amino Acid Sequence Bacillus / enzymology Biocatalysis Chitinases / chemistry Hydrogen-Ion Concentration Industrial Waste Sequence Alignment Temperature Waste Products
Acido-thermostable Bacillus altitudinis Chitin degradation Chitinase Endo-acting function Gene cloning

Journal

Carbohydrate research
ISSN: 1873-426X
Titre abrégé: Carbohydr Res
Pays: Netherlands
ID NLM: 0043535

Informations de publication

Date de publication:
Sep 2020
Historique:
received: 15 04 2020
revised: 26 06 2020
accepted: 28 06 2020
entrez: 19 8 2020
pubmed: 19 8 2020
medline: 1 6 2021
Statut: ppublish

Résumé

This paper reports the isolation and identification of an acido-thermostable chitinase (ChiA-Ba43) which was purified, from the culture liquid of Bacillus altitudinis strain KA15, and characterized. Purification of ChiA-Ba43 produced a 69.6-fold increase in the specific activity (120,000 U/mg) of the chitinase, with a yield of 51% using colloidal chitin as substrate. ChiA-Ba43 was found to be a monomeric protein with a molecular mass of 43,190.05 Da as determined by MALDI-TOF/MS. N-terminal sequence of the first 27 amino-acids (aa) of ChiA-Ba43 displayed homology to chitinases from other Bacillus species. Interestingly, ChiA-Ba43 exhibited optimum pH and temperature of 4-5.5 and 85 °C, respectively. Thin-layer chromatography (TLC) showed that the final hydrolyzed products of the enzyme from chitin-oligosaccharides and colloidal chitin are a mixture of (GlcNAc)

Identifiants

DOI: 10.1016/j.carres.2020.108089 PMID: 32807357
pubmed: 32807357
pii: S0008-6215(20)30244-5
doi: 10.1016/j.carres.2020.108089
pii:
doi:

Substances chimiques

Industrial Waste 0
Waste Products 0
Chitinases EC 3.2.1.14

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

108089

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

Auteurs

Katia-Louiza Asmani (KL)

Department of Biochemistry and Microbiology, Faculty of Biological and Agricultural Sciences (FBAS), University of Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou, 15000, Algeria. Electronic address: katia.asmani@yahoo.com.

Khelifa Bouacem (K)

Department of Biochemistry and Microbiology, Faculty of Biological and Agricultural Sciences (FBAS), University of Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou, 15000, Algeria; Laboratory of Cellular and Molecular Biology (LCMB), Microbiology Team, Faculty of Biological Sciences (FBS), University of Sciences and Technology of Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, Algiers, 16111, Algeria.

Akli Ouelhadj (A)

Department of Biochemistry and Microbiology, Faculty of Biological and Agricultural Sciences (FBAS), University of Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou, 15000, Algeria; Laboratory of Food Quality and Food Safety (LFQFS), Faculty of Biological and Agricultural Sciences (FBAS), University of Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou, 15000, Algeria.

Merzouk Yahiaoui (M)

Department of Natural and Life Sciences, Faculty of Sciences (FS), University of M'Sila, P.O. Box 166, M'Sila, 28000, Algeria.

Sofiane Bechami (S)

Department of Biochemistry and Microbiology, Faculty of Biological and Agricultural Sciences (FBAS), University of Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou, 15000, Algeria.

Sondes Mechri (S)

Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax, 3018, Tunisia.

Fadoua Jabeur (F)

Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax, 3018, Tunisia.

Kahina Taleb-Ait Menguellet (K)

Department of Biochemistry and Microbiology, Faculty of Biological and Agricultural Sciences (FBAS), University of Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou, 15000, Algeria.

Bassem Jaouadi (B)

Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax, 3018, Tunisia. Electronic address: bassem.jaouadi@cbs.rnrt.tn.

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Classifications MeSH

questionsmedicales.fr › Sciences de l'information › Sources d'information › Services d'information › Documentation › Données de séquences moléculaires › Séquence d'acides aminés › Biochemical and molecular characterization of...
questionsmedicales.fr › Bactéries › Bactéries à Gram positif › Bâtonnets à Gram positif › Bâtonnets sporulés à Gram positif › Bacillaceae › Bacillus › Biochemical and molecular characterization of...
questionsmedicales.fr › Métabolisme › Biocatalyse › Biochemical and molecular characterization of...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Glycosidases › Chitinase › Biochemical and molecular characterization of...
questionsmedicales.fr › Phénomènes chimiques › Concentration en ions d'hydrogène › Biochemical and molecular characterization of...
questionsmedicales.fr › Environnement et santé publique › Santé publique › Pollution de l'environnement › Déchets › Déchets industriels › Biochemical and molecular characterization of...
questionsmedicales.fr › Techniques d'investigation › Techniques génétiques › Alignement de séquences › Biochemical and molecular characterization of...
questionsmedicales.fr › Environnement et santé publique › Environnement › Concepts météorologiques › Atmosphère › Temps (météorologie) › Température › Biochemical and molecular characterization of...
questionsmedicales.fr › Environnement et santé publique › Santé publique › Pollution de l'environnement › Déchets › Biochemical and molecular characterization of...