The digestion in vitro of triglycerides by pancreatic lipase.

نویسندگان

  • F H MATTSON
  • L W BECK
چکیده

The formation of partial glycerides by the hydrolysis in vitro of triglycerides with pancreatic lipase was first reported by Artom and Reale (1) and then again several years later by Frazer and Sammons (2). In these studies apparently no attention was paid to the isomeric form of the digestion products. Desnuelle et al. (3) further studied the hydrolysis of triglycerides and showed it to be a series of stepwise reactions from triglyceride to diglyceride to monoglyceride to glycerol, fatty acid being released at each step. The quantitative aspects of this work were weakened by their supposition that the hydrolysis was a random one. The pertinent literature in this field has been the subject of an excellent review by Desnuelle (4). The hydrolysis in vivo of triglycerides was reported by this laboratory (5) to be a directed one from triglyceride to 1,2-diglyceride to 2-monoglyceride. Partial conversion of 2-monoglyceride to the 1 isomer also appeared to occur in the intestine. It was likewise reported that at the conclusion of hydrolysis in vitro only the 1 isomer of monoglyceride was present. Subsequently, Borgstriim (6), using methods never previously applied to these types of materials, reported that there is selective formation of 1,2-diglycerides and 2-monoglycerides when triglycerides are hydrolyzed in vitro with pancreatic lipase. In the studies reported here the course of hydrolysis in vitro was found to be the same as hydrolysis in vivo. From some of the characteristics of the reactions, it appears that lipase may be specific for the hydrolytic and esterification reactions occurring at the primary hydroxyl group positions of glycerol.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Does the pancreas really produce much more lipase than required for fat digestion?

Thirty years ago, it was reported that a linear relationship does not exist between the amounts of human pancreatic lipase secreted in chronic pancreatitis and the degree of steatorrhea, which was considered to appear only after more than 90% of the pancreatic secretory capacity had been lost. From these observations, it was generally thought that the lipolytic potential of the pancreas is much...

متن کامل

Studies on the effect of bile and lipolysis products on pancreatic lipase and colipase activity in vitro.

This study shows that human bile, at a concentration in the range of that found in the intestinal lumen, inhibited the hydrolysis of emulsified triolein by pancreatic lipase in vitro. The addition of colipase in excess to lipase failed to restore lipolytic activity. In contrast, a partially degraded emulsion of triolein containing diacylglycerol, monoacylglycerol and free fatty acid was hydroly...

متن کامل

In vitro model relating lipid digestibility and quality

A model system was established to evaluate the ability of a pancreatic lipase enzyme to hydrolyse fats and oils, simulating lipid digestion in vitro. Lipid hydrolysis was monitored by quantification of the level of free fatty acids, mono-, diand triglycerides. In the model system the pancreatic lipase was able to hydrolyse a non-oxidized fat quite rapidly. The activity of the lipase enzyme was ...

متن کامل

Angptl4 serves as an endogenous inhibitor of intestinal lipid digestion.

Dietary triglycerides are hydrolyzed in the small intestine principally by pancreatic lipase. Following uptake by enterocytes and secretion as chylomicrons, dietary lipids are cleared from the bloodstream via lipoprotein lipase. Whereas lipoprotein lipase is inhibited by several proteins including Angiopoietin-like 4 (Angptl4), no endogenous regulator of pancreatic lipase has yet been identifie...

متن کامل

The complete digestion of human milk triacylglycerol in vitro requires gastric lipase, pancreatic colipase-dependent lipase, and bile salt-stimulated lipase.

Gastric lipase, pancreatic colipase-dependent lipase, and bile salt-stimulated lipase all have potential roles in digestion of human milk triacylglycerol. To reveal the function of each lipase, an in vitro study was carried out with purified lipases and cofactors, and with human milk as substrate. Conditions were chosen to resemble those of the physiologic environment in the gastrointestinal tr...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 214 1  شماره 

صفحات  -

تاریخ انتشار 1955