A new halotolerant xylanase from Aspergillus clavatus expressed in Escherichia coli with catalytic efficiency improved by site-directed mutagenesis-Reference-Cited by-同舟云学术

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A new halotolerant xylanase from Aspergillus clavatus expressed in Escherichia coli with catalytic efficiency improved by site-directed mutagenesis

Published:2024-06-06 Issue:7 Volume:14 Page:
ISSN:2190-572X
Container-title:3 Biotech
language:en
Short-container-title:3 Biotech

Author:

Pasin Thiago M.^ORCID,Lucas Rosymar C.,de Oliveira Tássio B.,McLeish Michael J.,Polizeli Maria de Lourdes T. M.

Funder

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Fundação de Amparo à Pesquisa do Estado de São Paulo

Conselho Nacional de Desenvolvimento Científico e Tecnológico

National Institute of Science and Technology of the Bioethanol

Publisher

Springer Science and Business Media LLC

Link

https://link.springer.com/content/pdf/10.1007/s13205-024-04021-7.pdf

Reference52 articles.

1. Bhardwaj N, Verma VK, Chaturvedi V, Verma P (2020) Cloning, expression and characterization of a thermo-alkali-stable xylanase from Aspergillus oryzae LC1 in Escherichia coli BL21(DE3). Protein Expr Purif 168:105551

2. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

3. Carli S, Meleiro LP, Rosa JC, Moraes LAB, Jorge JA, Masui DC et al (2016) A novel thermostable and halotolerant xylanase from Colletotrichum graminicola. J Mol Catal B Enzym 133:S508–S517

4. Chakdar H, Kumar M, Pandiyan K, Singh A, Nanjappan K, Kashyap PL et al (2016) Bacterial xylanases: biology to biotechnology. 3 Biotech 6:150

5. Charalambous K, O’Reilly AO, Bullough PA, Wallace BA (2009) Thermal and chemical unfolding and refolding of a eukaryotic sodium channel. Biochim Biophys Acta 1788:1279–1286

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