Cell-bound lipase and esterase of Brevibacterium linens.
The activities of glycerol ester hydrolase, lipase (EC 3.1.1.3) and carboxylesterase, and esterase (EC 3.1.1.1) were determined for whole cell preparations of Brevibacterium linens by using the pH-stat assay. The culture growth liquors were inactive against the three substrates, tributyrin emulsion, triacetin, and methyl butyrate. Cells washed in water had less activity than cells washed in 5% NaCl; the ratio of activities was close to 1:2 for all strains using tributyrin emulsion as the substrate. For the esterase substrates, this relationship varied widely and was strain dependent. The ability to hydrolyze the two esterase substrates varied independently of the level of lipase activity.
D001951:Brevibacterium / Q000201:enzymology*; D002087:Butyrates / Q000378:metabolism; D002474:Cell-Free System; D002611:Cheese; D004950:Esterases / Q000378:metabolism*; D005516:Food Microbiology; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008049:Lipase / Q000378:metabolism*; D012965:Sodium Chloride / Q000494:pharmacology; D014215:Triacetin / Q000378:metabolism; D014280:Triglycerides / Q000378:metabolism; D014867:Water
D002087:Butyrates; D014280:Triglycerides; D014867:Water; D012965:Sodium Chloride; D004950:Esterases; D008049:Lipase; D014215:Triacetin