title: One step purification of peanut phospholipase D by precipitation with alginate.
abstract: A simple titrimetric assay with soybean lecithin has been used for screening phospholipase D activity from some plant sources, viz. peanut, wheat germ, cabbage and carrot. The enzyme from peanut has been purified by binding to alginate which is a water soluble polymer. The purification consisted of co-precipitation of enzyme with alginate upon addition of 0.06 M Ca++. The enzyme was eluted from the polymer using 0.2 M sodium chloride. The activity recovery was 61% with 34 fold purification.
authors.affiliation: Chemistry Department, Indian Institute of Technology, New Delhi, India.
authors.forename: S
authors.initials: S
authors.lastname: Sharma
authors.forename: A
authors.initials: A
authors.lastname: Sharma
authors.forename: M N
authors.initials: MN
authors.lastname: Gupta
mesh_terms: D000464:Alginates; D010367:Arachis / Q000201:enzymology*; D002122:Calcium Chloride; D011232:Chemical Precipitation; D020723:Glucuronic Acid; D006603:Hexuronic Acids; D010713:Phosphatidylcholines; D010739:Phospholipase D / Q000302:isolation & purification*; D012995:Solubility; D013379:Substrate Specificity
chemical_list: D000464:Alginates; D006603:Hexuronic Acids; D010713:Phosphatidylcholines; D020723:Glucuronic Acid; D010739:Phospholipase D; D002122:Calcium Chloride