Skip to Content
Merck

L8906

Lipase from Mucor javanicus

lyophilized powder, ≥300 units/mg solid (using olive oil)

Synonym(s):

Triacylglycerol acylhydrolase, Triacylglycerol lipase

Slide 1 of 1
Sign In to View Organizational & Contract Pricing.

Select a Size

1 G

2 160,00 kr

5 G

8 560,00 kr

2 160,00 kr

Please contact Customer Service for Availability
Request a Bulk Order

About This Item

CAS Number:
9001-62-1
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-619-9
EC Number:
3.1.1.3 (BRENDA, IUBMB)
MDL number:
MFCD00131509

Key Documents

View All Documentation

Skip To

Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

Lipase from Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)

InChI key

QWZUIMCIEOCSJF-CHHCPSLASA-N

InChI

1S/C11H9N3O2.Na/c15-8-4-5-9(10(16)7-8)13-14-11-3-1-2-6-12-11;/h1-7,16H,(H,12,14);/q;+1/b13-9-;

form

lyophilized powder

specific activity

≥300 units/mg solid (using olive oil)

storage temp.

2-8°C

Quality Level

100

Looking for similar products? Visit Product Comparison Guide

Compare Similar Items

View Full Comparison

Show Differences

1 of 4

This Item
623026230562285
Lipase from Mucor javanicus lyophilized powder, ≥300 units/mg solid (using olive oil)

Sigma-Aldrich

L8906

Lipase from Mucor javanicus

Sigma-Aldrich

Sigma-Aldrich

62302

Lipase from Candida rugosa

Lipase from Rhizopus oryzae powder (fine), ~10 U/mg

Sigma-Aldrich

62305

Lipase from Rhizopus oryzae

Lipase from Aspergillus oryzae lyophilized, powder, white, ~50 U/mg

Sigma-Aldrich

62285

Lipase from Aspergillus oryzae

specific activity

≥300 units/mg solid (using olive oil)

specific activity

15-25 U/mg

specific activity

~10 U/mg

specific activity

~50 U/mg

form

lyophilized powder

form

lyophilized solid, powder (fine)

form

powder (fine)

form

powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

Analysis Note

Protein determined by biuret.

Application

Lipase from Mucor javanicus can be used to catalyze the production of polyglycerol polyricinoleate from polyricinoleic acid and polyglycerol-3. [1]
Lipase from Mucor javanicus has been used in a study to assess the effects of lyophilization time and water content on the salt-induced activation of enzymes in organic solvents. [2]

Biochem/physiol Actions

Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

General description

Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols.

Other Notes

One unit will hydrolyze 1.0 microequivalent of fatty acid from a triglyceride in 1 hr at pH 7.7 at 37 °C using olive oil (30 minute incubation).

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
BCCC1786
BCBM5263V
BCBM5263
1431633V
1431633

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

M T Ru et al.
Biotechnology and bioengineering, 63(2), 233-241 (1999-04-01)
The addition of simple inorganic salts to aqueous enzyme solutions prior to lyophilization results in a dramatic activation of the dried powder in organic media relative to enzyme with no added salt. Activation of both the serine protease subtilisin Carlsberg
Hani El-Nezami et al.
Journal of agricultural and food chemistry, 52(14), 4577-4581 (2004-07-09)
Viable, heat-and acid-killed Lactobacillus rhamnosus strain GG (LGG) has shown high binding properties with zearalenone (ZEN). To identify the type of chemical moieties and interactions involved in binding with the ZEN, LGG was subjected to different chemical and enzymatical treatments
Screening and selection of lipases for the enzymatic production of polyglycerol polyricinoleate.
Bo?dalo, A.
Biochemical Engineering Journal, 46, 217-222 (2009)
C Guo et al.
Letters in applied microbiology, 55(6), 453-459 (2012-10-17)
This study aims to assess the removal mechanism of patulin using heat-treated Saccharomyces cerevisiae cells and identify the role of different cell wall components in the binding process. In order to understand the binding mechanism, viable cells, heat-treated cells, cell
Hidehiko Wakabayashi et al.
Journal of agricultural and food chemistry, 51(15), 4349-4355 (2003-07-10)
The enantioselectivity of the generation of 3-mercaptohexanal and 3-mercaptohexanol, two potent sulfur-containing aroma compounds, by lipase-catalyzed hydrolysis of the corresponding 3-acetylthioesters was investigated. The stereochemical course of the kinetic resolutions was followed by capillary gas chromatography using modified cyclodextrins as
View All Related Papers

Questions

Reviews

No rating value

Active Filters

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service