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Lipases break down triglycerides into glycerol and free fatty acids. They are the enzymes responsible for lipid metabolism, breaking down fats that are essential for energy and other biological functions. Lipases are found in a wide variety of species, from animals to plants, from fungi to bacteria and even archaea. Apart from their physiological functions, lipases have found widespread industrial and research applications due to their ability to initiate esterification and transesterification reactions under mild conditions, making them valuable tools in biotechnology.
Lipases are hydrolases—enzymes that cleave molecules with water. They generally operate between the water and lipid phases and can therefore easily target and hydrolyze hydrophobic substrates. This feature—interfacial activation—is unique to lipases and makes them highly catalytic. Lipases have received a lot of interest in recent years due to their stability and versatility in both aqueous and non-aqueous conditions. Creative Enzymes offers a variety of lipases to meet the needs of industrial manufacturing and biotechnological research.
The primary function of lipases is to catalyze the breakdown of triglycerides into free fatty acids and glycerol. This reaction is essential for several physiological processes, particularly energy metabolism. Lipases are secreted in the digestive system of animals, where they aid in the digestion of fat. In humans, the best-known lipase is pancreatic lipase, which is secreted into the small intestine to digest dietary fats.
Fig. 1: General enzymatic reaction of a lipase. Under natural conditions lipases catalyze the hydrolysis of triacylglycerol into a diglyceride and fatty acid. In non-aqueous environment, lipases can also catalyze ester synthesis (adapted from Jaeger et al., 1994).
In fat metabolism, lipases are involved in regulating the balance between fat storage and fat mobilization. Lipoprotein lipase (LPL) hydrolyzes triglycerides in circulating lipoproteins, allowing tissues such as muscle and fat to take up fatty acids for storage or energy production. Hormone-sensitive lipase (HSL) in adipose tissue essentially unlocks stored fat during fasting or increased energy consumption.
Fig. 2: Lipid metabolic pathways in the human body (Liu et al., 2020).
In addition to a metabolic function in lipid metabolism, lipases are unique to each species. Lipases in plants also mediate lipid signaling and membrane remodeling. Microbial lipases—lipases produced by bacteria and fungi—have adapted to function in diverse environments where microbes degrade lipids to acquire nutrients.
Lipases are diverse and can be classified based on their origin, structure, and substrate specificity. The three primary types are:
Lipases are widely used in the food industry, biofuel production and research where their specificity and efficiency are advantageous.
Lipases are widely used in the dairy industry to enhance the flavor of cheese. They break down milk fats and release free fatty acids that make cheeses such as blue cheese and parmesan delicious. Lipases are also found in baked goods and margarines, where they modify fats to improve texture and flavor.
Lipases are key ingredients in laundry and dishwashing detergents. They break down fats and oils at cold temperatures, so they're environmentally friendly and effective at removing grease stains from clothes and dishes. Detergent lipases are often bacterial and are engineered to be stable at different pH ranges.
Lipases are used in the production of biodiesel because they catalyze the transesterification of triglycerides to fatty acid methyl esters (FAME), one of the main components of biodiesel. Microbial lipases are ideal for biofuels because they are non-aqueous, providing a sustainable alternative to chemical catalysts.
Lipases are used in the pharmaceutical industry, which are necessary for the synthesis of enantiomerically pure drugs. Lipase-catalyzed reactions are highly specific and efficient, without harsh chemical reactions and can make drug synthesis more sustainable.
Lipases participate in bioremediation activities such as degrading lipid contaminants in wastewater and soil. They convert industrial wastewater containing fats, oils and greases into biodegradable materials. Lipase-based systems are already being developed to deal with oil spills and other environmental contaminants.
Fig. 3: Application of lipases in different industries (Vishnoi et al., 2020).
In summary, lipases are key enzymes with multiple functions in lipid metabolism, from fat metabolism to lipid storage and mobilization. Lipases have wide applications in food, biofuel and pharmaceutical industries due to their specialized, flexible and sustainable catalytic activity. In research studies, lipases remain invaluable for lipid metabolism and biotechnological advances.
Lipases | |||
Cat. No. | Product Name | Activity | Inquiry |
NATE-1752 | Native Aspergillus sp. Lipase (API) | 100,000 unit/g | Get a quote |
NATE-0400 | Native Chromobacterium viscosum Lipase | > 2,000 units/mg protein | |
NATE-0401 | Native Human Lipase | > 250 units/mg protein (Lowry) | |
NATE-0403 | Native Porcine Lipase | > 20,000 units/mg protein | |
NATE-0417 | Native Burkholderia sp. Lipoprotein Lipase | > 50,000 units/mg solid | |
NATE-1609 | Native Mucor miehei Lipase | > 4,000 units/mg | |
NATE-1638 | Monoglyceride lipase from Human, Recombinant |
> 170 units/mg |
Creative Enzymes offers a wide range of high-quality lipases from a variety of sources. Our lipases are carefully engineered to meet industry standards, ensuring optimal performance for each unique application. For more information or to discuss your specific needs, please don't hesitate to contact us today!
References:
Catalog | Product Name | EC No. | CAS No. | Source | Price |
---|---|---|---|---|---|
NATC-209 | Lipase for Biodiesel Production | Aspergillus nig... | Inquiry | ||
NATZ-046 | Native Aspergillus niger Lipase A | 9001-62-1 | Aspergillus nig... | Inquiry | |
NATZ-045 | Native Mucor javanicus Lipase M | 9001-62-1 | Mucor javanicus | Inquiry | |
NATE-1753 | Native Aspergillus sp. Lipase (immobilized) | EC 3.1.1.3 | 9001-62-1 | Aspergillus sp. | Inquiry |
NATE-1752 | Native Aspergillus sp. Lipase (API) | EC 3.1.1.3 | 9001-62-1 | Aspergillus sp. | Inquiry |
NATE-1638 | Monoglyceride lipase from Human, Recombinant | EC 3.1.1.23 | E. coli and fus... | Inquiry | |
NATE-1614 | Native Thermus flavus Lipase | EC 3.1.1.3 | 9001-62-1 | Thermus flavus | Inquiry |
NATE-1613 | Native Thermus thermophilus Lipase | EC 3.1.1.3 | 9001-62-1 | Thermus thermop... | Inquiry |
NATE-1612 | Native Rhizopus niveus Lipase | EC 3.1.1.3 | 9001-62-1 | Rhizopus niveus | Inquiry |
NATE-1611 | Lipase from Pseudomonas cepacia | EC 3.1.1.3 | 9001-62-1 | Pseudomonas cep... | Inquiry |
NATE-1610 | Native Aspergillus oryzae Lipase (Solution) | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-1609 | Native Mucor miehei Lipase | EC 3.1.1.3 | 9001-62-1 | Mucor miehei | Inquiry |
NATE-1608 | Native Aspergillus oryzae Lipase | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-1607 | Native Aspergillus niger Lipase | EC 3.1.1.3 | 9001-62-1 | Aspergillus nig... | Inquiry |
NATE-0406 | Lipase from Candida sp., Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-0399 | Native Candida rugosa Lipase | EC 3.1.1.3 | 9001-62-1 | Candida rugosa | Inquiry |
NATE-0404 | Native Rhizopus oryzae Lipase | EC 3.1.1.3 | 9001-62-1 | Rhizopus oryzae | Inquiry |
NATE-0403 | Native Porcine Lipase | EC 3.1.1.3 | 9001-62-1 | Porcine pancrea... | Inquiry |
NATE-0402 | Native Penicillium camemberti Lipase | EC 3.1.1.3 | 9001-62-1 | Penicillium cam... | Inquiry |
NATE-0401 | Native Human Lipase | EC 3.1.1.3 | 9001-62-1 | Human pancreas | Inquiry |
NATE-0400 | Native Chromobacterium viscosum Lipase | EC 3.1.1.3 | 9001-62-1 | Chromobacterium... | Inquiry |
NATE-0539 | Lipase−polyethylene glycol | Inquiry | |||
NATE-0417 | Native Burkholderia sp. Lipoprotein Lipase | EC 3.1.1.34 | 9004-02-8 | Burkholderia sp... | Inquiry |
NATE-0405 | Lipase from Candida sp., Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus nig... | Inquiry |
NATE-0398 | Lipase B from Candida Antarctica, Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-0397 | Lipase A from Candida Antarctica, Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |