Oat Lipase and Tributyrin

Intracellular hydrolysis of short chain glycerides by rat small intestine in vitro and transfer of glycerol

“…Thus the intestinal esterase did not necessarily show a different specificity, with regard to position of ester groups attached, from pancreatic lipase, which appears to be specific for the 1,3-ester linkages (Mattson & Volpenhein, 1966). However, Schonheyder & Volqvartz (1952) and Peers (1953) were able to detect partial glycerides as major products in their studies on the enzymic hydrolysis of short chain glycerides, suggesting that the absence of partial glycerides in the present experiments may indicate an enzymic mechanism in the hydrolysis of all three ester linkages.…”

A novel Geotrichum candidum lipase with some preference for the 2-position on a triglyceride molecule

“…Thin-layer chromatography of the enzyme reaction products obtained with triolein as substrate. Lanes 1-4, the hydrolytic products with lipase I; 7-10, the hydrolytic products with lipase IV; 5 and 11, 2-monoolein; 6 and 12, 1-monoolein; 13, 1,2(2,3)-diolein; 14, 1,3-diolein; 15, triolein; 16, oleic acid to be 1,3-specific (Sonnet 1988), the only exception being oat lipase, which was reported to be p r o b a b l y 2-specific (Peers 1953). In this sense, the newly isolated G. candidurn lipase IV would be an attractive enzyme with a unique positional specificity between 2-specific and non-specific.…”

The esteratic and chylolytic properties of post‐heparin plasma and their role in lipaemia clearing*

“…However, the work of Shore et al (1953) makes it appear unlikely that phospholipids or cholesterol esters are the source of these fatty acids. The actual substrate for the 'heparin-enzyme' maybe either neutral fats or lower glycerides formed earlier by the action of pancreatic lipase on the intestinal fat (Peers, 1953). SUMMARY 1.…”