| Identification | Back Directory | [Name]
Lipase | [CAS]
9001-62-1 | [Synonyms]
Lipase
lipazin
tweenase
meitomy30
amanon-ap
butyrinase
LIPASE MML
Accelerase
Lipase
plantlipase
tributyrase
Amidase 001
AlcalaseCLEA
LIPASELIQUID
LIPASEPOWDER
remzymepl600
triacetinase
PANCRELIPASE
LIPASE CAL-B
Fungallipase
ga56(enzyme)
LIPASE crude
Lipolase 100L
Lipase,fungal
tweenesterase
tributyrinase
LIPASE ENZYME
Nitrilase 002
Chitinase 001
LIPASEALKALINE
Lipase,porcine
takedo1969-4-9
tweenhydrolase
AMANO LIPASE M
AMANO LIPASE PS
LIPASE PS AMANO
LIPASE AS AMANO
LIPASE AK AMANO
Lipase(Candida)
LIPASE AYS AMANO
LIPASE, >4 U/MG*
LIPASE M AMANO 10
trioleinhydrolase
Palatase? 20,000L
Amano Lipase AYS
triglyceridelipase
tributyrinesterase
Lipase,Pseudomonas
Lipase froM Candida
froM Porcine Pancreas
tracylglycerol lipase
Triacylglycerollipaza
Nitrile Hydratase 001
triglyceridehydrolase
Lipase,triacylglycerol
glycerolesterhydrolase
lipase from wheat germ
lipase from aspergillus
lipase(fromhogpancreas)
lipase, porcine panreas
thermomyces lanuginosus
Lipase(pocine pancreas)
triacylglycerolhydrolase
LIPASE FROM MUCOR MIEHEI
Lipase, Triacylglycerin-
LIPASE CAL-A, THERMOSTABLE
LIPASE FROM HUMAN PANCREAS
LIPASE FROM CANDIDA RUGOSA
lipase from rhizopus oryzae
lipase from pseudomonas sp.
LIPASE FROM MUCOR JAVANICUS
PPL/Lipase(pocine pancreas)
NovoCat Lipase screening kit
lipase from burkholderia sp.
Haloalkane dehalogenase DhaA
Haloalkane dehalogenase DhlA
Lipase 002-CLEA(Isoform B)
Lipase from porcine pancreas
LIPASE TYPE I FROM WHEAT GERM
lipase from rhizomucor miehei
lipase from rhizopus arrhizus
lipase from aspergillus niger
Novozymes lipase, broad range
Lipase from Candida utilis
Lipase from Thermus flavus
NovoCat Protease screening kit
Lipase from Aspergillus sp.
Lipase form Candida antarctica
lipase from candida antarctica
LipaseExChromobacteriumViscosum
lipase from candida cylindracea
lipase from pseudomonas cepacia
Lipase from Rhizopus delemar
Lipase from Thermus aquaticus
lipase from pseudomonas stutzeri
LipaseExPigPancreas(E.C.3.1.1.3)
LIPASE FROM ASPERGILLUS ORYZAE*
LIPASE FROM MUCOR MIEHEI, ~1 U/MG
Lipase from Candida lipolytica
lipase from penicillium camemberti
lipase from penicillium roqueforti
LIPASE FROM MUCOR JAVANICUS, 5 U/G
LIPASE TYPE VII FROM CANDIDA RUGOSA
LIPASE FROM ASPERGILLUS, >0.5 U/MG*
lipase from thermomyces lanuginosus
LIPASE, REKOMBINANT AUS ASPERGILLUS
LIPASE AUS WEIZENKEIMEN, ~0.1 U/MG*
LIPASE FROM CANDIDA RUGOSA >2 U/MG*
Lipase from Thermus thermophilus
Protease/Peptidase of fungal origin
Novozymes lipase mutant, broad range
LIPASE FROM RHIZOPUS ARRHIZUS, 2 U/G
LIPASE AUS ASPERGILLUS NIGER, 4 U/G*
LIPASE FROM PSEUDOMONAS FLUORESCENS
LIPASE FROM THERMUS FLAVUS, ~0.7 U/G
lipase from chromobacterium viscosum
AMANO LIPASE M, FROM MUCOR JAVANICUS
Lipase NB from Burkholderia plantarii
LIPASE FROM RHIZOPUS ORYZAE ~12 U/MG*
LIPASE FROM CANDIDA LIPOLYTICA, 1 U/G
LIPASE, REKOMBINANT AUS MUCOR MIEHEI,
LIPASE TYPE XI FROM RHIZOPUS ARRHIZUS
LIPASE AUS THERMUS AQUATICUS, ~3 U/G*
LIPASE FROM CANDIDA UTILIS, ~0.1 U/MG
LIPASE FROM RHIZOPUS NIVEUS ~1.5 U/MG
AMANO LIPASE A, FROM ASPERGILLUS NIGER
LIPASE FROM ASPERGILLUS NIGER, ~1 U/MG
LIPASE TYPE VI-S FROM PORCINE PANCREAS
LipasefromPenicilliumroqueforti,>0.4umg
LIPASE FROM CANDIDA ANTARCTICA APPROX.
NovoCat Hydrolytic enzyme screening kit
Nitrilase 001 (recombinant in E. coli )
LIPASE FROM BURKHOLDERIA SP., ~12 U/MG*
LIPASE FROM RHIZOPUS DELEMAR, ~0.4 U/MG
Novozymes lipase from Rhizomucor miehei
LIPASE ACRYLIC BEADS FROM*CANDIDA RUGOSA
LIPASE FROM RHIZOMUCOR MIEHEI, ~0.5 U/MG
LIPASE, RECOMBINANT FROM MUCOR MIEHEI, E
LIPASE RECOMBINANT, FROM*THERMOMYCES LAN
LIPASE FROM CANDIDA CYLINDRACEA, ~2 U/MG
NovoCat Immobilized Lipase screening kit
AMANO LIPASE AK, FROM PSEUDOMONAS FLUORE
LIPASE FROM RHIZOPUS DELEMAR POWDER AP
AMANO LIPASE F-AP15 FROM RHIZOPUS &
LIPASE, RECOMBINANT, FROM*THERMOMYCES LA
LIPASE FROM ASPERGILLUS ORYZAE, ~50 U/MG
LIPASE, RECOMBINANT, FROM*RHIZOMUCOR MIE
amano lipase from pseudomonas fluorescens
NovoCat Immobilized Protease screening kit
Nitrilase CDX202 (recombinant in E. coli )
LIPASE FROM PSEUDOMONAS CEPACIA, ~50 U/M G
LIPASE TYPE XIII FROM PSEUDOMONAS*SPECIE S
Protease mixture from Streptomyces griseus
Novozymes lipase A from Candida antarctica
Novozymes lipase B from Candida antarctica
LIPASE FROM THERMUS THERMOPHILUS, ~0.6 U /G
LIPASE FROM HOG PANCREAS, POWDER, 15-35U/MG
LIPASE TYPE II CRUDE FROM*PORCINE PANCRE AS
LIPASE FROM PENICILLIUM ROQUEFORTI ~150 U/G
LIPASE FROM HOG PANCREAS, LYOPH., ~1 00 U/MG
lipase acrylic resin from candida antarctica
Lipase from porcine pancreas, PS Lipase
Novozymes lipase from Thermomyces lanuginosus
Amano Lipase F-AP15 from Rhizopus oryzae
Lipase from Rhizomucor miehei,Palatase 20,000L
LIPASE FROM PENICILLIUM CAMEMBERTI 5 U/G*
LIPASE TYPE XII FROM CHROMOBACTERIUM*VIS COSUM
Amano Lipase PS, from Burkholderia cepacia
Lipase [from porcine pancreas, >=20000 units/mg]
LIPASE FROM PSEUDOMONAS FLUORESCENS, ~35 00 U/MG
LIPASE FROM PSEUDOMONAS FLUORESCENS, ~40 U/MG*
LIPASE FROM CANDIDA ANTARCTICA, LYOPH., ~0.5 U/MG
Lipase–Agarose 4% beaded agarose. from wheat germ
LIPASE NB RESEARCH GRADEFROM PSEUDOMONAS PLANTARII
LIPASE FROM PSEUDOMONAS FLUORESCENS, ~300 U/MG*
LIPASE FROM CANDIDA CYLINDRACEA, LYOPH., ~30 U/MG
NovoCat Immobilized Hydrolytic enzyme screening kit
Lipase from Penicillium camemberti,Lipase G50 Amano
AMano Lipase A froM Aspergillus niger >=120,000 U/g
LIPASE FROM HOG PANCREAS, LYOPH., POWDER , ~100 U/MG
Novozymes lipase from Thermomyces lanuginosus, mutant
Triacylglycerol acylhydrolase, Triacylglycerol lipase
Lipase acrylic resin from Candida antarctica,Novozym 435
LIPASE B, RECOMBINANT FROM CANDIDA ANT-A RCTICA, ~9 U/MG
LIPASE A CANDIDA ANTARTICA, REC. FROM ASP. ORYZAE ~2 U/MG
Lipase-Macroporous acrylic beads from Candida rugosa
lipase rhizomucor miehei, recombinant from aspergillus oryzae
PPL, Triacylglycerol acylhydrolase, Triacylglycerol lipase
Lipase Mucor miehei, recombinant from Aspergillus oryzae
Lipase from Candida antarctica, type B (Covalently immobilized)
lipase b candida antarctica, recombinant from aspergillus oryzae
Lipase A Candida antarctica, recombinant from Aspergillus oryzae
AMano Lipase froM PseudoMonas fluorescens beige-brown, >=20,000 U/g
PS Lipase, Triacylglycerol acylhydrolase, Triacylglycerol lipase
Lipase modified by directed evolution for large substrates, stereoselective
Esterase Kit (Esterase 001, 002, 003, 004, 006, 007, 008, 009, 011, 002-CLEA)
Lipase from Mucor miehei,Triacylglycerol acylhydrolase, Triacylglycerol lipase
Lipase from human pancreas,Triacylglycerol acylhydrolase, Triacylglycerol lipase
Lipase from Candida rugosa,Triacylglycerol acylhydrolase, Triacylglycerol lipase
Lipase from Mucor javanicus,Triacylglycerol acylhydrolase, Triacylglycerol lipase | [EINECS(EC#)]
232-619-9 | [Molecular Formula]
n.a. | [MDL Number]
MFCD02685890 | [MOL File]
9001-62-1.mol | [Molecular Weight]
238.198 |
| Chemical Properties | Back Directory | [Appearance]
powder | [density ]
1.2 | [vapor pressure ]
0.004Pa at 25℃ | [storage temp. ]
2-8°C
| [solubility ]
H2O: 2 mg/mL, hazy with insoluble particles, faintly yellow
| [form ]
solution
| [color ]
yellow-brown
| [Stability:]
Moisture sensitive. Incompatible with strong oxidizing agents. | [Water Solubility ]
It is soluble in water. | [Merck ]
13,5533 | [CAS DataBase Reference]
9001-62-1 | [EPA Substance Registry System]
Lipase, triacylglycerol(9001-62-1) |
| Hazard Information | Back Directory | [Chemical Properties]
powder | [Uses]
To split fats without damaging sensitive constituents, such as vitamins or unsaturated fatty acids. In food processing for flavor improvement; in detergents for the improvement of cleaning action. For review of industrial applications of microbial lipases, see Seitz, J. Am. Oil Chem. Soc. 51, 12 (1974). | [Definition]
lipase: An enzyme secreted by thepancreas and the glands of the smallintestine of vertebrates that catalysesthe breakdown of fats into fatty acidsand glycerol. | [General Description]
Pancrelipase (Cotazym) has agreater lipolytic action than other pancreatic enzyme preparations.Hence, it is used to help control steatorrhea and inother conditions in which pancreatic insufficiency impairsthe digestion of fats in the diet. | [Flammability and Explosibility]
Notclassified | [Biochem/physiol Actions]
Amano lipase M is capable of catalyzing Michael addition of pyrimidine with disaccharide acrylates in organic media. |
| Questions And Answer | Back Directory | [Description]
Lipase is an enzyme and belongs to the class of hydrolase. Lipase is produced in the pancreas, mouth, and stomach. It catalyzes the hydrolysis of triglycerides to glycerol and free fatty acids. The body uses lipase to break down fats in food so they can be absorbed in the intestines.
Lipases are widely employed to catalyze hydrolysis, alcoholysis, esterification, interesterification, acidolysis and transesterification of carboxylic esters. Their unique characteristics include substrate specificity, stereospecificity, regioselectivity and ability to catalyze a heterogeneous reaction at the interface of water soluble and water insoluble systems. Lipases are used as flavor and aroma constituents in the food industry, to produce valuable oleo chemical species for diesel engines, as additives in cosmetic formulations, to remove the pitch from pulp produced in the paper industry, for the hydrolysis of milk fat in the dairy industry, to remove non-cellulosic impurities from raw cotton before further processing into dyed and finished products, for the drug formulations in the pharmaceutical industry, and to remove subcutaneous fat in the leather industry. Lipases are also used to diagnose pancreatitis in patients. Clinically lipases help a person who has cystic fibrosis, Alzheimer's disease, atherosclerosis and act as a candidate target for cancer prevention and therapy. Lipases are also used to treat obesity in recent years.
| [References]
[1] http://www.umm.edu/health/medical/altmed/supplement/lipase
[2] Tianwei Tan, Jike Lu, Kaili Nie, Li Deng, Fang Wang (2010) Biodiesel production with immobilized lipase: A reveiw, 28, 628-634
[3] G. D. Haki, S. K. Rakshit (2003) Developments in industrially important thermostable enzymes: a rview, 89, 17-34
[4] Jack M. Goldberg (1976) Diagnostic use of pancreatic lipase determination by radial enzyme diffusion, and design of a routine pancreatic profile, 22, 638-642
[5] H. Loli, SK. Narwal, NK. Saun, R. Gupta (2015) Lipases in medicine: an overview, 15, 1209-1216
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