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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

An Antarctic Bacillus sp. isolate was found to exhibit extracellular α-galactosidase activity. On the basis of the results of 16S rRNA sequencing, the strain was named Bacillus sp. LX-1. In a one-factor-at-a-time experiment, galactose, peptone and Mn 2+ were found to be the medium components that facilitated enzyme production. The new strain showed optimal α-galactosidase activity at pH 7.0 and temperature of 40°C. The enzyme exclusively hydrolyzed α-D-galactosides such as p-nitrophenyl--galactopyranoside, melibiose, raffinose and stachyose, and showed no effect with proteases such as trypsin, pancreatin, and pronase. Enzyme activity was almost completely inhibited by the presence of Ag + , Hg 2+ , Cu 2+ , and sodium dodecylsulfate (SDS) but was unaffected by β-mercaptoethanol and ethylenediaminetetraacetic acid (EDTA). The LX-1 α-galactosidase may be a promising candidate as a biocatalyst for soybean processing in food and feed industries. Key words: Antarctic, Bacillus sp., α-galactosidase, one-factor-at-a-time, biocatalyst.

Production and partial characterization of α-galactosidase activity from an Antarctic bacterial isolate, Bacillus sp. LX-1