Open AccessA novel isoprimeverose‐producing enzyme from Phaeoacremonium minimum is active with low concentrations of xyloglucan oligosaccharides
Author(s) -
Matsuzawa Tomohiko,
Kameyama Akihiko,
Yaoi Katsuro
Publication year - 2019
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12549
Subject(s) - xyloglucan , glycoside hydrolase , aspergillus oryzae , chemistry , polysaccharide , biochemistry , oligosaccharide , cellobiose , enzyme , cell wall , hydrolysis , disaccharide , cellulase
Xyloglucan is one of the major polysaccharides found in the plant cell wall and seeds. Owing to its complex branched structure, several different hydrolases are required to degrade it. Isoprimeverose‐producing enzymes (IPase) are unique among the glycoside hydrolase 3 family in that they recognize and release a disaccharide from the nonreducing end of xyloglucan oligosaccharides. Only two IP ases have been previously isolated and characterized. A novel IP ase from Phaeoacremonium minimum (Pm IP ase) was expressed and characterized. The xylopyranosyl residue at the nonreducing end of xyloglucan oligosaccharides was essential for hydrolytic activity, and Pm IP ase was unable to hydrolyze cellobiose into d ‐glucose. Pm IP ase had a K m for xyloglucan oligosaccharide substrate that was much lower than that of the reported IPase isolated from Aspergillus oryzae . This indicates that Pm IP ase was able to produce isoprimeverose efficiently from low concentrations of xyloglucan oligosaccharides. Pm IP ase also exhibited transglycosylation activity and was able to transfer isoprimeverose units to its substrates.