Hydrolysis of fully esterified alcohols containing from one to eight hydroxyl groups by the lipolytic enzymes of rat pancreatic juice.
The enzymatic hydrolysis in vitro of the esters of methanol, ethylene glycol, glycerol, erythritol, pentaerythritol, adonitol, sorbitol, and sucrose in which all alcohol groups were esterified with oleic acid was studied. Various preparations of rat pancreatic juice, including pure lipase, were used as the sources of enzymes. Lipase (EC 3.1.1.3) did not hydrolyze compounds that contained more than three ester groups. Compounds containing four and five ester groups were hydrolyzed by certain preparations of pancreatic juice; this activity is attributed to the enzyme, nonspecific lipase. This enzyme also hydrolyzed esters of primary alcohols. The compounds containing six (sorbitol) and eight (sucrose) ester groups were not hydrolyzed.
D000818:Animals; D001646:Bile / Q000201:enzymology; D001647:Bile Acids and Salts; D002918:Chymotrypsin; D004896:Erythritol; D004950:Esterases; D004952:Esters; D005990:Glycerol; D006018:Glycols; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000037:antagonists & inhibitors; D000432:Methanol; D009829:Oleic Acids; D010189:Pancreatic Juice / Q000201:enzymology*; D011409:Propylene Glycols; D051381:Rats; D013012:Sorbitol; D013395:Sucrose
D001647:Bile Acids and Salts; D004952:Esters; D006018:Glycols; D009829:Oleic Acids; D011409:Propylene Glycols; D013012:Sorbitol; D013395:Sucrose; D004950:Esterases; D008049:Lipase; D002918:Chymotrypsin; D005990:Glycerol; D004896:Erythritol; D000432:Methanol