Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2020 May 1:150:662-670.
doi: 10.1016/j.ijbiomac.2020.02.126. Epub 2020 Feb 13.

Characterization of a novel bifunctional mannuronan C-5 epimerase and alginate lyase from Pseudomonas mendocina. sp. DICP-70

Ming Sun  1 , Chu Sun  2 , Tang Li  3 , Kuikui Li  3 , Shenggang Yan  4 , Heng Yin  5
Affiliations

Characterization of a novel bifunctional mannuronan C-5 epimerase and alginate lyase from Pseudomonas mendocina. sp. DICP-70

Ming Sun et al. Int J Biol Macromol. .

Abstract

Alginate is a family of industrially important linear polymers consisting of β-D-mannuronic acid (M) and its C-5 epimer α-L-guluronic acid (G). The function of alginate is closely related to the ratio of M/G. Mannuronan C-5 epimerase, which converts M to G, is a key enzyme involved in the biosynthesis of alginate. A new mannuronan C-5 epimerase isolated from Pseudomonas mendocina. sp. DICP-70 named PmC5A was characterized in this study. From the 1H NMR analysis of the products, we have found that PmC5A possesses alginate lyase function in addition to mannuronan C-5-epimerase. The optimal pH and temperature of lyase and epimerase were found to be 8.0, 9.0 and 40 °C, 30 °C, respectively. PmC5A also shows lyase activity toward PolyMG and G-blocks.

Keywords: Alginate; Alginate lyase; Mannuronan C-5 epimerase.

PubMed Disclaimer

MeSH terms

LinkOut - more resources