Lipase

Base Information

• Chemical Name: Lipase
• CAS No.: 9001-62-1
• Molecular Formula: Unspecified
• Molecular Weight: 238.19783
• Hs Code.: 35079020
• Mol file: 9001-62-1.mol

Synonyms:ABSFungal Lipase L;Lipase PF;Lipase PL 266;Lipase PLG;Lipase PN;Lipase PS;Lipase PS Amano SD;Acid lipase;Adipose triglyceride lipase;Alfamalt LP 10066;Allzyme Lipase;Altus 13;Altus 2;Amano AP;Amano AY 1;Amano B;Amano CE;Amano CES;Amano I;Amano II;Amano LPL 200S;Amano M;Amano N-AP;Amano P;Amano PS 30;Arthrobacter lipase;Bakezyme PH 800;Bile salt-activated lipase;Bioprase OP 10;Butyrinase;Buzyme 2517;Cacordase;Capalase;Capalase K;Capalase L;Cartazyme LP;Chirazyme 435;Chirazyme L;Chirazyme L 1;Chirazyme L 10;Chirazyme L 2;Chirazyme L2C2;Chirazyme L 3;Chirazyme L 5;Chirazyme L 6;Chirazyme L 7;Chirazyme L 8;Chirazyme L 9;Chirazyme c-f;ChiroCLEC-CAB;ChiroCLEC-CR;ChiroCLEC-PC;Cleanase NLA-P;CloneZyme ESL 001;E.C.3.1.1.3;Enzylon PF;Fetipase;Fluozim G 3Kh;GA 56;GA 56(enzyme);Glycerol ester hydrolase;Greasex;Greasex 100L;ICR-107;ICR-113;Italase;Italase C;Lilipase A 10;Lilipase A 10FG;Lilipase A 5;Lilipase B 2;Lillipase A-10FG;Lipase;Lipase A;Lipase A 100L;Lipase A 10FG;Lipase AH;Lipase AK Amano;Lipase AKG;Lipase ALC;Lipase ALG;Lipase AP;Lipase AS;Lipase AY;Lipase AY 30;Lipase AY Amano 6;Lipase CE;Lipase CR;Lipase D Amano 2000;Lipase D Amano 350;Lipase EU-034;Lipase GC Amano 4;Lipase L Amano 10;Lipase LAK;Lipase LP;Lipase LP 'S';Lipase M 10;Lipase M-AP 10;Lipase MY;Lipase OF;Lipase OFEX;Lipase PA;

Chemical Property of Lipase

Chemical Property:

• Appearance/Colour: yellow-brown solution
• Vapor Pressure: 0.004Pa at 25℃
• Density: 1.2
• Storage Temp.: 2-8°C
• Solubility.: H2O: 2 mg/mL, hazy with insoluble particles, faintly yellow
• Water Solubility.: It is soluble in water.

Purity/Quality:

99% ^*data from raw suppliers

LipaseAY30 ^*data from reagent suppliers

Safty Information:

• Pictogram(s): B,Xn
• Hazard Codes: B,Xn
• Statements: 20/21/22
• Safety Statements: 22-24/25-36/37-36

MSDS Files:

SDS file from LookChem

Useful:

• General Description: Lipase is a versatile enzyme that catalyzes the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. It plays a critical role in lipid metabolism, digestion, and energy storage, with applications in food processing, detergents, pharmaceuticals, and biotechnology. Lipases are produced by various sources, including animals, plants, and microorganisms (e.g., fungi and bacteria), and exhibit substrate specificity, pH, and temperature optima depending on their origin. Some lipases, such as those from *Amano* or *Chirazyme* series, are commercially optimized for industrial use, while others like bile salt-activated lipase and adipose triglyceride lipase have specialized physiological functions. Their ability to function in both aqueous and non-aqueous environments makes them valuable for synthetic chemistry, including esterification and transesterification reactions.

Technology Process of Lipase

There total 2 articles about Lipase which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:

Reference yield: 95.0%

→ (S)-(-)-2,3-dihydro-3-(4'-hydroxyphenyl)-1,1,3-trimethyl-1H-inden-5-ol + lipase (9001-62-1)

Guidance literature:

Reference yield: 73.5%

→ (S)-decan-2-ol (33758-16-6) + lipase (9001-62-1)

Guidance literature:

Reference yield:

1-hexadecylcarboxylic acid (57-10-3) + lipase (9001-62-1) + hexan-1-ol (111-27-3) → isooctyl palmitate (106-05-8)

Guidance literature:

Downstream raw materials:

isooctyl palmitate

Refernces

Enzymatic synthesis of both enantiomers of 2-methylene-4- (fluoromethyl)-4-butanolides

10.1021/jo981183z

The research aims to develop efficient methods for synthesizing chiral 2-methylene-4-(fluoromethyl)-4-butanolides, which are important due to their potential biological activities and applications in optical devices. The study explores two main synthetic routes: enzymatic lactonization and kinetic resolution. Key chemicals used include 5,5,5-trifluoro (or 5,5-difluoro)-4-hydroxy-2-methylenepentanoic acid as a starting material, lipases such as lipase PS and lipase MY for enzymatic reactions, and vinyl acetate for esterification. The researchers achieved high enantioselectivity in the synthesis of both enantiomers, obtaining (R)-2a and (S)-2a with 96% and 97% ee respectively, and (R)-2b and (S)-2b with 97% and 98% ee respectively. The study concludes that by carefully selecting lipases and controlling reaction conditions, highly optically pure products can be obtained efficiently, overcoming limitations such as low yield and long reaction times associated with previous approaches.

Enzymatic preparation of cis and trans-3-amino-4-hydroxytetrahydrofurans and cis-3-amino-4-hydroxypyrrolidines

10.1016/j.bmc.2014.05.014

The study focuses on the enzymatic preparation and resolution of cis and trans-3-amino-4-hydroxytetrahydrofurans and cis-3-amino-4-hydroxypyrrolidines, which are important heterocyclic amino alcohols found in bioactive natural products and drugs. The researchers utilized Candida antarctica lipases A and B as catalysts in hydrolytic processes to achieve high enantioselectivity for these heterocycles. The study successfully assigned the absolute configurations of the optically pure heterocycles obtained and demonstrated a convenient biocatalytic approach for preparing all isomers of these compounds. The findings have implications for the synthesis of complex molecules with potential biological activities, as well as for applications in organocatalysis and as chiral auxiliaries.

10.1016/0006-3002(52)90066-8

The study investigates the enzymatic hydrolysis of tripropionyl glycerol by liver esterase and pancreatic lipase. Liver esterase rapidly cleaves one acid group from tripropionyl glycerol, forming 1,2-dipropionyl glycerol, which then preferentially releases the propionyl group in position 1 at a slower rate, ultimately yielding 2-monopropionyl glycerol that decomposes very slowly. Pancreatic lipase, however, converts tripropionyl glycerol into 1,2-dipropionyl glycerol, with the reaction nearly halting thereafter. The study also synthesizes various propionyl glycerols and other propionyl esters to elucidate the hydrolysis pathway and the impact of ester structure on hydrolysis rates, revealing that free hydroxyl groups, especially primary ones, significantly inhibit enzyme activity.