LIPASE

CAS NUMBER: 9001-62-1

EC NUMBER: 232-619-9

Lipase is any enzyme that catalyzes the hydrolysis of fats (lipids). 
Lipases are a subclass of the esterases.
Lipases perform essential roles in digestion, transport and processing of dietary lipids (e.g. triglycerides, fats, oils) in most, if not all, living organisms. 
Genes encoding lipases are even present in certain viruses.
Most lipases act at a specific position on the glycerol backbone of a lipid substrate. 
For example, human pancreatic lipase (HPL), which is the main enzyme that breaks down dietary fats in the human digestive system, converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids.
Several other types of lipase activities exist in nature, such as phospholipases and sphingomyelinases; however, these are usually treated separately from "conventional" lipases.
Some lipases are expressed and secreted by pathogenic organisms during an infection. 
In particular, Candida albicans has many different lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.

Lipase is an enzyme that breaks down triglycerides into free fatty acids and glycerol. 
Lipases are present in pancreatic secretions and are responsible for fat digestion. 
There are many different types of lipases; for example, hepatic lipases are in the liver, hormone-sensitive lipases are in adipocytes, lipoprotein lipase is in the vascular endothelial surface, and pancreatic lipase in the small intestine. 
Understanding lipase is crucial for understanding the pathophysiology of fat necrosis and is clinically significant in the understanding of acute and chronic pancreatitis. 
The role of lipase is also crucial in the mechanism of some medications indicated for lowering cholesterol. 
This review will explore the function, pathophysiology, and clinical significance of the lipase enzyme.
Lipase catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids. 
Its function is important for digestion and promoting absorption of fats in the intestines. 
Lipase is primarily found in and secreted by the pancreas, but is also found in the saliva and stomach.

Lipase is a digestive enzyme that is found in many plants, animals, bacteria, and molds. 
An enzyme is a protein that speeds up a particular biochemical reaction in the body. 
People use lipase as a medicine.
A lipase test measures the amount of this enzyme in a blood sample. 
High amounts of lipase may be found in the blood when the pancreas is damaged or when the tube leading from the pancreas (pancreatic duct) to the beginning of the small intestine is blocked.
Lipase is one type of hydrolytic enzymes responsible for degrading or modifying nonpolar (e.g. triglycerides) and polar lipids (e.g. galactolipids and phospholipids) found in both animal and plant sources.
Lipases are key enzymes involved in fat digestion in humans and animals by converting insoluble triacylglycerols into more soluble products, fatty acids and mono-acylglycerols, that can easily be metabolized for energy generation.
Lipase is an enzyme the body uses to break down fats in food so they can be absorbed in the intestines. 
Lipase is produced in the pancreas, mouth, and stomach. 
Most people produce enough pancreatic lipase, but people with cystic fibrosis, Crohn disease, and celiac disease may not have enough lipase to get the nutrition they need from food.

Lipase is a digestive enzyme that is found in many plants, animals, bacteria, and molds. 
An enzyme is a protein that speeds up a particular biochemical reaction in the body. 
People use lipase as a medicine.
Enzymes are becoming an increasingly important component of detergents as consumers seek ways to easily and effectively clean a range of stains with minimal damage to fabrics and the environment. 
Some enzymes are already widely used in detergents to remove a variety of common stains:

Proteases remove human sweat, blood and egg.
Amylases remove starch residues from chocolate, gravies and pasta.
Cellulases brighten the color of cotton blends and soften the fabric by modifying the fabric’s structure.
Lipases, though, represent the most important group of biocatalysts in the biotechnology industry because of their commercial potential. 
They’re biodegradable, non-toxic, easy to produce in large quantities and tailorable for a variety of substrates.

Lipase is one type of enzyme. 
Enzymes are protein molecules that work as catalysts to speed up a reaction. 
They act specifically, meaning that each enzyme only works on a particular molecule. 
For example, lipase binds to fatty substances but would not bind to sugary compounds.
Enzymes do not get used up during a reaction and can act as a catalyst repeatedly. 
One enzyme can usually catalyze about 10,000 reactions per second.
Only a small amount of enzyme can produce a large effect on the solution because each enzyme is reusable so many times. 
Most detergents contain only 0.4 to 0.8 percent crude enzyme by weight.

Lipase is the enzyme that breaks down lipids (fats).
Most act at a specific location along the glycerol chain so different lipases can target specific types of fats. 
Using a specific selection of lipases on a substrate can also create a particular final product.
Several human and industrial lipases exist. 
The human pancreas produces lipases as part of the digestion process. 
Animals, bacteria and fungi also produce lipases. 
Lipases used for industrial purposes were once procured from animal sources, though now they’re primarily sourced from bacteria and fungi. 
Research has begun into engineering enzymes for specific applications.
Lipase is used for indigestion, heartburn, allergy to gluten in wheat products (celiac disease), Crohn's disease, and cystic fibrosis.
Along with lipase, the pancreas secretes insulin and glucagon, two hormones the body needs to break down sugar in the bloodstream. 
Other pancreatic enzymes include amylase, which breaks down a certain starch into its sugar building blocks, and protease, which breaks down protein into single amino acids.
Lipase can be found in many plants and animals. 
In recent decades, lipases have been produced commercially from highly specialized microorganisms such as bacteria, yeast and fungi.

FUNCTION:

Lipase is an enzyme that breaks down triglycerides into free fatty acids and glycerol. 
Lipases are present in pancreatic secretions and are responsible for fat digestion. 
Lipases are enzymes that play a crucial role in lipid transport. 
There are many different types of lipases; hepatic lipases are in the liver, hormone-sensitive lipases are in adipocytes, lipoprotein lipase is in the vascular endothelial surface, and pancreatic lipase is in the small intestine, each serving individual functions. 
Hepatic lipase in the liver is responsible for degrading the triglycerides that remain in intermediate density lipoprotein (IDL). 
Hormone-sensitive lipase is found within fat tissue and is responsible for degrading the triglycerides that are stored within adipocytes. 
Lipoprotein lipase is found on the vascular endothelial surface and is responsible for degrading triglycerides that circulating from chylomicrons and VLDLs. 
Pancreatic lipase is found within the small intestine and is responsible for degrading dietary triglycerides. 
Hepatic lipase plays a crucial role in the formation and delivery of low-density lipoprotein(LDL). 

Lipase is formed by the modification of intermediate density lipoprotein in the peripheral tissue and liver by hepatic lipase. 
These Lipase particles are taken up, or endocytosed, via receptor-mediated endocytosis by target cell tissue. 
Lipase serves to ultimately transport cholesterol from the liver to peripheral tissue.
Lipases catalyze hydrolytic reactions of lipids by cleaving the carboxylic ester bonds between the glycerol backbone and one or more of the fatty acid chains.
The term ’lipase’ is usually expressed as a singular noun although it encompasses different types of lipolytic enzymes. The following table lists lipases which perform essential functions in baked goods, such as foam emulsification (i.e. gas bubble stabilization) and crumb softening through starch complexing.
Lipases act on the endogenous lipids found in wheat flour and other lipids added in the form of oil or lecithin. 
Flour lipids are a complicated mixture of compounds. Of the 2.0–3.0% (w/w) lipid material found in whole wheat flour, about 50% are non-polar lipids (triacyl glycerides, fatty acids, sterols, and their esters), and the other half are strongly polar (phospholipids and galactolipids).

USES:

Most people do not need additional lipase. 
However, people with the following conditions may find lipase supplements helpful.
Lipase is used for indigestion, heartburn, allergy to gluten in wheat products (celiac disease), Crohn's disease, and cystic fibrosis.
Several applications already use lipases, including pharmaceuticals, leather, bioremediation, agriculture, cosmetics and detergents. 
Each year, approximately 1,000 tons of lipases make their way into detergents, though it still only accounts for less than 5 percent of the detergent market. 
Lipase use in the cosmetic and detergent industry could grow 9.13 percent annually.
More specifically, lipases, usually in conjunction with other substances, are used in detergents that remove manure from domestic animals, as well as in water reconditioning and degreasing. 
They’re also a component of cleaning products used in the foodservice industry to unclog drains and grease traps.
Enzymatic cleaning of medical instruments before they undergo disinfection is also typical. 

Lipase detergent can help remove the biofilm left on gastrointestinal endoscopes and difficult stains and particles left on orthopedic and laparoscopic surgical instruments. 
They also clean delicate instruments used for microsurgical ophthalmic procedures.
The automotive industry uses lipase to process biodiesel, changing vegetable oil into fuel. 
This use makes it a desirable alternative for costlier, energy-intensive chemicals. 
The commercial food industry uses lipases to produce cheese and yogurt, and research is investigating its use in baking.

-Skin conditioner 
-cleansing agent 
-anti-acne 
-anti-cellulite 
-anti-dandruff

USES AND EFFECTIVENESS:

-Allergy to gluten in wheat products (celiac disease).
-Crohn's disease.
-Indigestion.
-Heartburn.
-Nausea and vomiting
-Diarrhea
-Severe back pain
-Severe abdominal pain
-Fever
-Loss of appetite
-A family history of pancreatitis
-Diabetes
-Gallstones
-High triglycerides
-Obesity
-Other conditions.

INDUSTRIAL USES:

Lipases serve important roles in human practices as ancient as yogurt and cheese fermentation. 

DIAGNOTIC USES:

Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas. 
Measured serum lipase values may vary depending on the method of analysis.

MEDICAL USES:

Lipase can also assist in the breakdown of fats into lipids in those undergoing pancreatic enzyme replacement therapy (PERT). 
Lipase is a key component in Sollpura (Liprotamase).

APPLICATION:

Lipases, as stand alone ingredients, do not replace emulsifiers. 
They need proper conditions to function and a sufficient amount of substrate to render the desired effect on the dough or batter. 
For dough strengthening purposes and foam emulsification, the key aspect about lipases is that they transform polar lipids into functional lysolipids which have superior surface activity, higher HLB value and a greater capacity to absorb at oil/water or/and gas/liquid interfaces.
Like  other enzymes, lipases require special conditions for optimum activity and performance, namely:

-Acidity (pH): Most lipases prefer rather alkaline conditions (i.e. a pH of 8.0), so higher doses are needed to obtain equivalent functionality.
-Temperature: Most lipases prefer temperatures above 45°C (113°F). Chemical reaction rates double for every 10°C (18°F) increase in temperature.
-Enzyme-substrate contact time.
-Sufficient water activity to support chemical reaction.
-Amount of substrate (enzymes work better when there is excess substrate).
-Adequate enzyme dosage (excess FFA may result in a rancid taste). Lipase overdose could also lead to a breakdown of the in-situ produced lysolipids, increasing the risk of gas bubble coalescence and rupture, and eventually a loss of oven spring.

HOW DOES IT WORK:

Although science has known about lipase for a while, only recently have researchers found lipases that were suitable for use in detergents. 
Lipases have to meet the following qualities to be effective in a detergent:

-Active at low temperatures
-Stable at high temperatures
-Active in alkaline conditions (pH of eight or above)
-Stable in the presence of other additives likely to exist in the final product, such as metal ions, surfactants and oxidants.
-Gentle on skin.
-Lipase is an additive to detergents. The enzyme breaks down the oily stain, then surfactants in the detergent attach to the remnants of the stain to remove it from the clothing.

Lipase can be used on the surface of materials to ensure easy removal of oil. 
Lipase works by forming a fabric-lipase complex on the surface of the clothing that creates a barrier. 
The barrier stops the enzyme from being removed during washing and prevents oily substances from being deposited on the material. 
Lipase remains active once the clothing is dry.

PHYSICAL AND CHEMICAL PROPERTIES:

-Appearance: Beige powder
-Activity: ca. 100,000 U/g powder
-Molecular weight: 4.5
-Optimum pH: 8 - 9.5
-pH stability: 7 - 10
-Optimum temperature: 50 ºC
-Thermal stability: Below 40 ºC
-Inhibitors: Cationic detergents

STRUCTURE:

A diverse array of genetically distinct lipase enzymes are found in nature, and they represent several types of protein folds and catalytic mechanisms. 
However, most are built on an alpha/beta hydrolase fold and employ a chymotrypsin-like hydrolysis mechanism using a catalytic triad consisting of a serine nucleophile, a histidine base, and an acid residue, usually aspartic acid.

PHYSIOLOGICAL DISTRIBUTION:

Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling[14] and inflammation. 
Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces.
In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome.
Other lipase enzymes, such as pancreatic lipases, are secreted into extracellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body.
Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium (or in examples of pathogenic microbes, to promote invasion of a new host).
Certain wasp and bee venoms contain phospholipases that enhance the effects of injury and inflammation delivered by a sting.
As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology.
Malassezia globosa, a fungus thought to be the cause of human dandruff, uses lipase to break down sebum into oleic acid and increase skin cell production, causing dandruff.

PRECAUTIONS:

Side effects may include nausea and stomach upset. 
High doses of lipase may exacerbate symptoms of cystic fibrosis. 
Scientists do not know enough about the effects of lipase during pregnancy or breastfeeding, so speak with your doctor before taking lipase.

SYNONYM:

195833-46-6
1-O-(2,3-didodecoxypropyl) 5-O-(6-methyl-7-oxophenoxazin-3-yl) pentanedioate
DTXSID90583514
Lipase Substrate, >=95% (HPLC)