English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In this study, we report the purification and characterization of the extracellular protease BPP-B from the zein-utilizing Bacillus pumilus strain MS-1. The purified BPP-B exhibited glutamyl endopeptidase activity. The Optimum pHs for the cleavage of casein and Suc-Ala-Ala-Pro-Glu-pNA were 11.0 and 8.0, respectively. The bppB gene encoded a 303-amino-acid pre-pro form of BPP-B, and mature BPP-B contained 215-amino-acid residues. BPP-B had three V8 serine protease family signatures (amino acid residues 96-113, 120-137, and 211-224), a serine protease (trypsin or chymotrypsin) family signature (amino acid residues 120-136), and the catalytic triad of serine proteases (His135, Asp186 and Ser259). These results indicate that BPP-B is a glutamyl endopeptidase belonging to peptidase family S2B. This is the first report on a glutamyl endopeptidase from a Bacillus pumilus strain. Although we have recently reported a subtilisin-like protease (BPP-A) playing a major part in zein degradation by Bacillus pumilus strain MS-1, it is possible that BPP-B is also involved in the further digestion of zein.

Purification and molecular characterization of glutamyl endopeptidase from zein-utilizing Bacillus pumilus strain MS-1