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

A recombinant chitinase was purified from the cell extract of Escherichia coli JM109 transformed by plasmid pUC19 carrying the gene encoding family 19 chitinase of Streptomyces sp. J-13-3 by column chromatography on DEAE-Sepharose, CM-Sepharose, and Bio-Gel P-100. The final preparation was homogenous in polyacrylamide gel electrophoresis. The molecular weight of the purified enzyme was estimated to be 32,000. The recombinant chitinase hydrolyzed the trimer to hexamer of N-acetylglucosamine and had the identical N-terminal amino acid sequence of the mature protein, indicating removal of the signal sequence by E. coli signal peptidase. The fungal growth in well (200 microl of medium) of microplate by measurement of absorbance at 595 nm indicated that the chitinase (10 microg) completely and half inhibited growth of Trichoderma reesei and Aspergillus niger respectively.

bioscience, biotechnology, and biochemistry

Purification and Antifungal Activity of Recombinant Chitinase from<i>Escherichia coli</i>Carrying the Family 19 Chitinase Gene of<i>Streptomyces</i>sp. J-13-3

Purification and Antifungal Activity of Recombinant Chitinase fromEscherichia coliCarrying the Family 19 Chitinase Gene ofStreptomycessp. J-13-3