Efficient secretory expression of an alkaline pectate lyase gene from Bacillus subtilis in E. coli and the purification and characterization ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-03

AUTHORS

Bin Zhuge, Guo-Cheng Du, Wei Shen, Jian Zhuge, Jian Chen

ABSTRACT

The gene encoding pectate lyase (PL) from Bacillus subtilis WSHB04-02 was amplified by PCR, fused with a periplasmic secretion signal peptide sequence, pelB, from pET22b(+), cloned and expressed in Escherichia coli cells using a temperature control vector, pHsh. The recombinant E. coil was grown in a 5 l fermentor. PL was secreted in broth at 22 U l(-1) after 20 h when temperature was increased from 30 degrees C to 42 degrees C. The recombinant enzyme was purified to homogeneity as judged by SDS-PAGE. It was optimally active at pH 9.4 and 50 degrees C over 30 min. Analysis of polygalacturonic acid (PGA) degradation products by electrospray ionization (ESI)-mass spectrometry (MS) indicated that PL produced a mixture of unsaturated oligo-galacturonides including unsaturated tri-galacturonic acid and unsaturated bi-galacturonic acid but not unsaturated mono-galacturonic acid. More... »

PAGES

405-410

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-006-9249-6

DOI

http://dx.doi.org/10.1007/s10529-006-9249-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000385028

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17237974


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