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L4777

Sigma-Aldrich

Lipase acrylic resin

greener alternative

≥5,000 U/g, recombinant, expressed in Aspergillus niger

Synonym(s):

Novozyme 435

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About This Item

CAS Number:
9001-62-1
Enzyme Commission number:
3.1.1.3 (BRENDA, IUBMB)
EC Number:
232-619-9
MDL number:
MFCD00217536
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Aspergillus niger

form

solid

specific activity

≥5,000 U/g

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

matrix

macroporous acrylic resin

application(s)

diagnostic assay manufacturing

greener alternative category

Enabling,

storage temp.

2-8°C

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-;

InChI key

QWZUIMCIEOCSJF-CHHCPSLASA-N

General description

Lipases belong to the class of hydrolases. Microbes of plant and animal basis mainly produce lipase enzyme. It can also be produced by marine organisms.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biodiesel research. For more information see the article in biofiles.
Lipase from produced by submerged fermentation of a genetically modified Aspergillus niger microorganism and adsorbed on a macroporous resin.

Application

Lipase acrylic resin has been used:
  • as a catalyst to carry out the esterification of pLACT with butyric acid
  • as an additive in fully hydrogenated canola oil (FHCO) and high oleic sunflower oil (HOSO) blend for enzymatic interesterification
  • to study its effect on the degree of oleic acid conversion upon esterification

Immobilized preparation of a thermostable lipase, particularly useful in the synthesis of esters and amides, and has a broad substrate specificity.

Biochem/physiol Actions

Lipases are used in detergent, food, leather, pharmaceutical and dairy industries. It has several characteristics like substrate specificity, stereospecificity and regioselectivity. It also participates in various bioconversion reactions like, hydrolysis, esterification, acidolysis and aminolysis. Candida antarctica lipase B is considered as an important enzyme due to its use in esterification, hydrolysis, aminolysis and transesterification.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Covalent immobilization of Candida antarctica lipase B on nanopolystyrene and its application to microwave-assisted esterification
Bukhari A, et al.
Chinese Journal of Catalysis, 35(9), 1555-1564 (2014)
Gurpur Rakesh D Prabhu et al.
Nature protocols, 15(3), 925-990 (2020-01-31)
Since the advent of modern science, researchers have had to rely on their technical skills or the support of specialized workshops to construct analytical instruments. The notion of the 'fourth industrial revolution' promotes construction of customized systems by individuals using
Filippo Fabbri et al.
International journal of molecular sciences, 22(16) (2021-08-28)
In the present work, different hydrolases were adsorbed onto polypropylene beads to investigate their activity both in short-esters and polyesters synthesis. The software MODDE® Pro 13 (Sartorius) was used to develop a full-factorial design of experiments (DoE) to analyse the
Lipase: An Industrial Enzyme Through Metagenomics (2018)
Chemical and enzymatic interesterification of tristearin/triolein-rich blends: Chemical composition, solid fat content and thermal properties
Ahmadi L, et al.
European Journal of Lipid Science and Technology, 1014-1024 (2008)
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