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

Alkaline proteases from the digestive tract of anchovy were partially purified by ammonium sulfate fractionation, dialysis and Sephadex G-75 gel filtration. The purification fold and yield were 6.23 and 4.49%, respectively. The optimum activities of partially purified alkaline proteases were observed at 60°C and at pH 11.0. The alkaline proteases were stable within the temperature range of 40 to 50°C and pH range of 9.0 to 11.0. They were inhibited by the serine-protease inhibitor phenylmethylsulfonyl fluoride (PMSF) and trypsin specific inhibitor benzamidine, but were not inhibited by the β-mercaptoethanol. The enzymes were slightly activated by metal ions such as Na + and Ba 2+ and inhibited by Cu 2+ , Zn 2+ , K + and Mn 2+ at different degrees. The molecular weight of the partially purified enzyme was 24 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Key words : Alkaline proteases, Engraulis encrasicholus , purification, characterization, digestive tract.

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract