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Lipase

E ssentially a water- soluble enzyme , Lipase catalyzes the hydrolysis reaction taking place in the ester bonds of water–insoluble, lipid substrates. They are classified under the subclass, esterases . Lipase is an important enzyme as it aids in the digestion process along with the transport as well as processing of dietary lipids - particularly the. triglycerides , fats and oils in most living beings. Some g enes encoding lipases are also found in few viruses. Researches reveal that there are many types distinctive lipase enzymes found in nature. They differ from each other on the basis of protein folds and catalytic reactions that they represent and support. Also most of these lipase enzymes are built on an alpha-beta hydrolase linkages and function on chymotrypsin -like hydrolysis reaction which involve a serine nucleophile , an acid residue which is mainly aspartic acid and a histidine .

Distribution of Lipase :

  • The lysosomal lipase, as its name suggests is mainly found in an organelle called the lysosome and hence it name.
  • Pancreatic lipases are secreted in the extracellular spaces of the cells. Their main function here is to break down dietary lipids into simpler substances so as to ease the digest process as well as their transport all over the body.
  • Certain fungi and bacteria also produce lipases in order to facilitate the absorption of nutrients from external mediums.
  • Lipases tend to play an essential role in cell biology , as they are present in the biological membranes which are primarily composed of phospholipids .
  • Malassezia globosa , a fungus which causes human dandruff is known to employ lipase for breaking down the sebum into oleic acid which accentuates the production of skin cells, there by causing dandruff.

Benefits :

Lipases are mainly responsible for the break down of fats into simpler substances and easing the process of digestion in the intestines. This process is carried out by lipases breaking down triglycerides and oils for better absorption. They also help the body to utilize omega fatty acids in a better way.

References :

Svendsen A (2000). "Lipase protein engineering". Biochim Biophys Acta 1543 (2): 223–228. PMID   11150608 .

Afonso C, Tulman E, Lu Z, Oma E, Kutish G, Rock D (1999). "The genome of Melanoplus sanguinipes entomopoxvirus". J Virol 73 (1): 533–52. PMID   9847359 .

Girod A, Wobus C, Zádori Z, Ried M, Leike K, Tijssen P, Kleinschmidt J, Hallek M (2002). "The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity". J Gen Virol 83 (Pt 5): 973–8. PMID   11961250 .

Winkler FK, D'Arcy A, and W Hunziker (1990). "Structure of human pancreatic lipase". Nature 343 (6260): 771–774. doi : 10.1038/343771a0 . PMID   2106079 .

Diaz, B.L., and J. P. Arm. (2003). "Phospholipase A(2)". Prostaglandins Leukot Essent Fatty Acids 2-3 : 87–97. doi : 10.1016/S0952-3278(03)00069-3 . PMID   12895591 .

Goñi F, Alonso A (2002). "Sphingomyelinases: enzymology and membrane activity". FEBS Lett 531 (1): 38–46. doi : 10.1016/S0014-5793(02)03482-8 . PMID   12401200 .