当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Characterization of a novel bifunctional mannuronan C-5 epimerase and alginate lyase from Pseudomonas mendocina. sp. DICP-70.

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

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Sun M,Sun C,Li T,Li K,Yan S,Yin H

doi

10.1016/j.ijbiomac.2020.02.126

subject

Has Abstract

pub_date

2020-05-01 00:00:00

pages

662-670

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)38952-4

journal_volume

150

pub_type

杂志文章

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