Molecular cloning and purification of an endochitinase from Serratia marcescens (Nima) View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-10

AUTHORS

Alejandro Ruiz-Sanchez, Ramon Cruz-Camarillo, Ruben Salcedo-Hernandez, Jorge E. Ibarra, Jose Eleazar Barboza-Corona

ABSTRACT

An endochitinase gene from the Serratia marcescens Nima strain (chiA Nima) was cloned, sequenced, and expressed in Escherichia coli DH5αF′, and the recombinant protein (ChiA Nima) was purified by hydrophobic interaction chromatography. chiA Nima contains an open reading frame (ORF) that encodes an endochitinase with a deduced molecular weight and an isoelectric point of 61 kDa and 6.84, respectively. A sequence at the 5′-end was identified as a signal peptide, recognized by Gram-negative bacteria transport mechanism. Comparison of ChiA Nima with other chitinases revealed a modular structure formed by the catalytic domain and a putative chitin-binding domain. The purified chitinase was able to hydrolyze both trimeric and tetrameric fluorogenic substrates, but not a chitobiose analog substrate. ChiA Nima showed high enzymatic activity within a broad pH range (pH 4.0–10.0), with a peak activity at pH 5.5. The optimal temperature for enzymatic activity was detected at 55°C. More... »

PAGES

103-111

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1385/mb:31:2:103

DOI

http://dx.doi.org/10.1385/mb:31:2:103

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027143880

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16170210


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