Biochemical characterisation of a PL24 ulvan lyase from seaweed-associated Vibrio sp. FNV38
Biochemical characterisation of a PL24 ulvan lyase from seaweed-associated Vibrio sp. FNV38
复制标题
DOI:
10.1007/s10811-023-03136-3
复制
发表时间:
2023-12-07
影响因子:
3.3
通讯作者:
Adams,Jessica M. M.
中科院分区:
文献类型:
--
作者:
Rodrigues,Valerie J.;Jouanneau,Diane;Adams,Jessica M. M.
Ulvan is a green macroalgal cell wall polysaccharide that has tremendous potential for valorisation due to its unique composition of sulphated rhamnose, glucuronic acid, iduronic acid and xylose. Several potential applications such as production of biofuels, bioplastics and other value-added products necessitate the breakdown of the polysaccharide to oligomers or monomers. Research on ulvan saccharifying enzymes has been continually increasing over the last decade, with the increasing focus on valorisation of seaweed biomass for a biobased economy. Lyases are the first of several enzymes that are involved in saccharifying the polysaccharide and several ulvan lyases have been structurally and biochemically characterised to enable their effective use in the valorisation processes. This study investigates the whole genome ofVibriosp.FNV38, an ulvan metabolising organism and biochemical characteristics of a PL24 ulvan lyase that it possesses. The genome ofVibriosp.FNV38 has a diverse CAZy profile with several genes involved in the metabolism of ulvan, cellulose, agar, and alginate. The enzyme exhibits optimal activity at pH 8.5 in 100 mM Tris–HCl buffer and 30 °C. However, its thermal stability is poor with significant loss of activity after 2 h of incubation at temperatures above 25 °C. Breakdown product analysis reveals that the enzyme depolymerised the polysaccharide predominantly to disaccharides and tetrasaccharides.