Characteristics of polygalacturonate lyase C from Bacillus subtilis 7-3-3 and its synergistic action with PelA in enzymatic degumming.
An alkaline polygalacturonate lyase (PGL) from Bacillus subtilis 7-3-3, PelC, with diverse depolymerization abilities for different pectin substrates was found. The PGL activity of PelC decreased with increasing degree of methyl esterification of the substrate. PelA and PelC displayed notable synergistic effects in the enzymatic degumming of ramie fibers. Gum loss rates increased by 62% when PelC was used to replace up to three-eighths of the PelA dose (PelC, 60 U g(-1) ramie fibers). To the best of our knowledge, this study is the first to report the synergistic action of members of polysaccharide lyase families 1 and 3, represented by PelA and PelC, respectively. The present paper provides new insights into the improvement and production of enzymes used in enzymatic degumming.
State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, P. R. China.
Mouyong
M
Zou
Xuezhi
X
Li
Jian
J
Zhao
Yinbo
Y
Qu
D001412:Bacillus subtilis / Q000145:classification / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D032402:Boehmeria / Q000737:chemistry; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D010802:Phylogeny; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
D001426:Bacterial Proteins; D011133:Polysaccharide-Lyases; C023911:pectate lyase