Lipase

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

JW 642 inhibits MAGL in mouse, rat, human brains (IC50: 7.6, 14, 3.7 nM).

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

Porcine pancreatic lipase is an enzyme that has been shown to have antioxidative properties. It is used as an additive in biodiesel production, where it prevents the formation of trans fatty acids and reduces the amount of free radicals. This enzyme has been shown to have lipase, protease, and amylase activities by using surface methodology. Porcine pancreatic lipase can be used for the treatment of autoimmune diseases such as multiple sclerosis and rheumatoid arthritis. This enzyme interacts with other enzymes such as lipases, proteases, and amylases to catalyze reactions on surfaces. It can be used for asymmetric synthesis by hydrogen bonding or by forming an intermediate complex with metal ions.

JZP-430 is an effective, highly selective, irreversible inhibitor of α/β-hydrolase domain 6 (ABHD6) (IC50: 44 nM).

Lipase 09 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 35-55°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 09 was shown to hydrolyze p-Nitrophenyl esters of acetate (18 % activity compared to octanoate), butyrate (80 %), octanoate (100 %) and capate (40 %).

Lipase 65 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30-40°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 65 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (87 %), laurate (5 %), palmitate (0.2 %) and stearate (0.1 %).

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

Cymit Quimica's Phospholipase D 040 Halal and Kosher Food grade bulk enzyme (EPLD840.6). With one of the most competitive activity rates on the global market and manufactured in Europe, this enzyme is perfect for use in food, diagnostic, therapeutic and nutraceutical industries worldwide.  Phospholipase D is an enzyme that is expressed in almost all types of organisms and whose activity can be harnessed to synthesize critical raw materials, for example phosphatidylserine. Phosphatidylserine has shown itself to be an important functional ingredient in reducing cognitive dysfunction and dementia in the field of nutraceuticals. As a Halal and Kosher food grade enzyme, Cymit Quimica's Phospholipase D is an excellent candidate for a diverse variety of food industry applications. Furthermore our enzyme can be used in diagnostic assays, creating first-class drug delivery systems and APIs.

Lipase 32 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 50-70°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 32 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (88 %), laurate (11 %), palmitate (0.3 %) and stearate (0.1 %).

Lipase 31 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 40-80°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 31 was shown to hydrolyze p-Nitrophenyl esters of acetate (100 % activity) and butyrate (23 %).

Lipase 15 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 25°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 15 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (13 %), laurate (1 %), palmitate (1 %), stearate (<1 %), arachidate (<1 %) and behenate (<1 %).

JJKK 048 is a potent and selective MAGL inhibitor.

Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).

MJN110 (Cravatt Reagent) is a potent and selective MAGL inhibitor. MJN110 Produces Opioid-Sparing Effects in a Mouse Neuropathic Pain Model.

Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.

Lipase 04 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 60-70°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 04 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (68 %), laurate (2 %), palmitate (2 %), stearate (2 %), arachidate (2 %) and behenate (2 %).

NF-1819: strong, selective MGL inhibitor; eases MS symptoms; analgesic; penetrates brain with high permeability.

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.