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

D -Galactose-specific  L -arabinose isomerase (L-AI) would have much potential for the enzymatic conversion of  D -Galactose into D-tagatose, while most of the reported L-AIs are  L -arabinose specific. This study explored a highly  D -Galactose-specific L-AI from  Bifidobacterium adolescentis  (BAAI) for the production of D-tagatose. In the comparative protein-substrate docking for  D -Galactose and  L -arabinose, BAAI showed higher numbers of hydrogen bonds in  D -Galactose-BAAI bonding site than those found in  L -arabinose-BAAI bonding site. The activity of BAAI was 24.47 U/mg, and it showed good stability at temperatures up to 65°C and a pH range 6.0–7.5. The  K  m ,  V  max , and  K  cat / K  m  of BAAI were found to be 22.4 mM, 489 U/mg and 9.3 mM –1  min –1 , respectively for  D -Galactose, while the respective values for  L -arabinose were 40.2 mM, 275.1 U/mg, and 8.6 mM –1  min –1 . Enzymatic conversion of  D -Galactose into D-tagatose by BAAI showed 56.7% conversion efficiency at 55°C and pH 6.5 after 10 h.

Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production