Difference between revisions of "Lipase"

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== Description ==
 
== Description ==
  
A group of enzymes that hydrolyze fats ([http://cameo.mfa.org/materials/fullrecord.asp?name=triglyceride triglycerides]) to produce [http://cameo.mfa.org/materials/fullrecord.asp?name=glycerol glycerol] and [http://cameo.mfa.org/materials/fullrecord.asp?name=fatty%20acid fatty acids]. In nature, lipases are used in the digestion of foods and they are found in the pancreas as well as in many [http://cameo.mfa.org/materials/fullrecord.asp?name=mold%20%28fungus%29 molds], [http://cameo.mfa.org/materials/fullrecord.asp?name=fungus fungi], and bacteria. The optimum conditions for most enzyme activity is a temperature between 35 and 37C and a pH of 5-6. Lipase can be deactivated by most organic solvents with the exception of [http://cameo.mfa.org/materials/fullrecord.asp?name=ligroin ligroin]. Lipase is activated by the addition of small amounts of acid (ascorbic, [http://cameo.mfa.org/materials/fullrecord.asp?name=acetic%20acid acetic], [http://cameo.mfa.org/materials/fullrecord.asp?name=formic%20acid formic], [http://cameo.mfa.org/materials/fullrecord.asp?name=oxalic%20acid oxalic], [http://cameo.mfa.org/materials/fullrecord.asp?name=hydrochloric%20acid hydrochloric], [http://cameo.mfa.org/materials/fullrecord.asp?name=sulfuric%20acid sulfuric], etc.). Lipases are added to detergents to improve cleaning action. Lipases have also been shown to be effective for the cleaning of some [http://cameo.mfa.org/materials/fullrecord.asp?name=oil%20varnish oil varnishes]. (Wolbers, et al. 1990)
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A group of enzymes that hydrolyze fats ([[triglyceride|triglycerides]]) to produce [[glycerol]] and [[fatty acid|fatty acids]]. In nature, lipases are used in the digestion of foods and they are found in the pancreas as well as in many [[mold (fungus)|molds]], [[fungus|fungi]], and bacteria. The optimum conditions for most enzyme activity is a temperature between 35 and 37C and a pH of 5-6. Lipase can be deactivated by most organic solvents with the exception of [[ligroin]]. Lipase is activated by the addition of small amounts of acid (ascorbic, [[acetic acid|acetic]], [[formic acid|formic]], [[oxalic acid|oxalic]], [[hydrochloric acid|hydrochloric]], [[sulfuric acid|sulfuric]], etc.). Lipases are added to detergents to improve cleaning action. Lipases have also been shown to be effective for the cleaning of some [[oil varnish|oil varnishes]]. (Wolbers, et al. 1990)
  
 
== Synonyms and Related Terms ==
 
== Synonyms and Related Terms ==

Revision as of 13:35, 21 January 2014

Description

A group of enzymes that hydrolyze fats (triglycerides) to produce Glycerol and fatty acids. In nature, lipases are used in the digestion of foods and they are found in the pancreas as well as in many molds, fungi, and bacteria. The optimum conditions for most enzyme activity is a temperature between 35 and 37C and a pH of 5-6. Lipase can be deactivated by most organic solvents with the exception of Ligroin. Lipase is activated by the addition of small amounts of acid (ascorbic, acetic, formic, oxalic, hydrochloric, sulfuric, etc.). Lipases are added to detergents to improve cleaning action. Lipases have also been shown to be effective for the cleaning of some oil varnishes. (Wolbers, et al. 1990)

Synonyms and Related Terms

triacyglycerol lipase

CAS 9001-62-1

Hazards and Safety

Sensitive to moisture. May decompose in water. Contact may cause irritation.

Fisher Scientific: MSDS

Additional Information

R. Wolbers, N. Sterman, C. Stavroudis, "Notes for Workshop on New Methods in the Cleaning of Paintings", Getty Conservation Institute, Los Angeles, 1990.

Authority

  • Richard S. Lewis, Hawley's Condensed Chemical Dictionary, Van Nostrand Reinhold, New York, 10th ed., 1993
  • The Merck Index, Susan Budavari (ed.), Merck Research Labs, Whitehouse Station, NJ, 12th Edition, 1996 Comment: entry 5338
  • Richard C. Wolbers, Nanette T. Sterman, Chris Stavroudis, Notes for Workshop on New Methods in the Cleaning of Paintings, J.Paul Getty Trust, Los Angeles, 1990
  • Teri Hensick, contributed information, 1998

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