Glycerol ester hydrolase activity of lactic acid bacteria.
Seventeen strains of lactic acid bacteria were assayed for their glycerol ester hydrolase activity by using an improved agar-well technique, and eight strains by determining the activity in cell-free extracts using a pH-stat procedure. All cultures tested showed activity and hydrolyzed tributyrin more actively than they did tricaproin. The cell extract studies demonstrated that the cells contained intracellular esterases and lipases. The culture supernatant fluid was without activity. The lipase and the esterase differed in their relative activity to each other in the different extracts and in the ease by which they could be freed from the cellular debris. It is suggested that the lipase of these organisms is an endoenzyme and the esterase an ectoenzyme.
D002474:Cell-Free System; D005989:Glycerides / Q000378:metabolism; D007778:Lactobacillus / Q000201:enzymology*; D007934:Leuconostoc / Q000201:enzymology*; D008049:Lipase / Q000378:metabolism*; D010376:Pediococcus / Q000201:enzymology*; D013291:Streptococcus / Q000201:enzymology*
D005989:Glycerides; D008049:Lipase