Welcome to LookChem.com Sign In|Join Free


  • or


Post Buying Request

10024-47-2 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

10024-47-2 Usage

General Description

Isobutyl oleate is a chemical compound formed by the esterification of isobutyl alcohol and oleic acid. It is commonly used as a solvent, emollient, and dispersing agent in cosmetic and personal care products. Isobutyl oleate can also be found in industrial products such as lubricants, coatings, and adhesives. It is a clear, colorless liquid with a mild odor and is considered safe for use in consumer products when used in accordance with regulations and guidelines. Isobutyl oleate is known for its ability to improve the spreadability and texture of formulas, as well as provide a smooth, non-greasy feel on the skin.

Check Digit Verification of cas no

The CAS Registry Mumber 10024-47-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,0,0,2 and 4 respectively; the second part has 2 digits, 4 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 10024-47:
42 % 10 = 2
So 10024-47-2 is a valid CAS Registry Number.



According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 10, 2017

Revision Date: Aug 10, 2017


1.1 GHS Product identifier

Product name 2-methylpropyl (Z)-octadec-9-enoate

1.2 Other means of identification

Product number -
Other names Oelsaeure-isobutylester

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only. Lubricants and lubricant additives
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:10024-47-2 SDS

10024-47-2Relevant articles and documents

The 3D model of the lipase/acyltransferase from Candida parapsilosis, a tool for the elucidation of structural determinants in CAL-A lipase superfamily

Subileau, Maeva,Jan, Anne-Hélène,Nozac'h, Hervé,Pérez-Gordo, Marina,Perrier, Véronique,Dubreucq, Eric

, p. 1400 - 1411 (2015)

Abstract Because lipids are hydrophobic, the development of efficient bioconversions in aqueous media free of organic solvents is particularly challenging for green oleochemistry. Within this aim, enzymes exhibiting various abilities to catalyze acyltransfer reaction in water/lipid systems have been identified. Among these, CpLIP2 from Candida parapsilosis has been characterized as a lipase/acyltransferase, able to catalyze acyltransfer reactions preferentially to hydrolysis in the presence of particularly low acyl acceptor concentration and high thermodynamic activity of water (aw > 0.9). Lipase/acyltransferases are thus of great interest, being able to produce new esters at concentrations above the thermodynamic equilibrium of hydrolysis/esterification with limited to no release of free fatty acids. Here, we present a 3D model of CpLIP2 based on homologies with crystallographic structures of Pseudozyma antarctica lipase A. Indeed, the two enzymes have 31% of identity in their primary sequence, yielding a same general structure, but different catalytic properties. The quality of the calculated CpLIP2 model was confirmed by several methods. Limited proteolysis confirmed the location of some loops at the surface of the protein 3D model. Directed mutagenesis also supported the structural model constructed on CAL-A template: the functional properties of various mutants were consistent with their structure-based putative involvement in the oxyanion hole, substrate specificity, acyltransfer or hydrolysis catalysis and structural stability. The CpLIP2 3D model, in comparison with CAL-A 3D structure, brings insights for the elucidation and improvement of the structural determinants involved in the exceptional acyltransferase properties of this promising biocatalyst and of homologous enzymes of the same family.

Studies on the lipase-catalyzed esterification of alkyl oleates in solvent-free systems

Zhong, Hui,Fang, Zheng,Zou, Baohua,Li, Xin,Ouyang, Pingkai,Guo, Kai

, p. 114 - 117 (2013)

The alkyl oleates were prepared by esterification of oleic acid with alkyl alcohols catalyzed by the lipase from Candida sp. 99-125 in solvent-free system. The influence of several factors, including enzyme concentration, temperature, molar ratio between oleic acid and alkyl alcohols, the structure of alcohols and water content, was also investigated. The results indicated that the reactions catalyzed by Candida sp. lipase at 20 °C, in the presence of 5% (w/w) lipase, on the molar ratio of 1:1 between oleic acid and alcohols, afforded products in high yield and showed high selectivity to primary alcohols. The enzymatic synthesis gave purer products, compared with the conventional chemical synthesis. The lipase from Candida sp. 99-125 was identified to be an effective catalyst in the esterification of alcohol and oleic acid at low temperature.

Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes

Jan, Anne-Hélène,Dubreucq, éric,Subileau, Maeva

, p. 941 - 950 (2017/05/26)

The lipases/acyltransferases homologous to CpLIP2 of Candida parapsilosis efficiently catalyze acyltransfer reactions in lipid/water media with high water activity (aW>0.9). Two new enzymes of this family, CduLAc from Candida dubliniensis and CalLAc8 from Candida albicans, were characterized. Despite 82 % sequence identity, the two enzymes have significant differences in their catalytic behaviors. In order to understand the roles played by the different subdomains of these proteins (main core, cap and C-terminal flap), chimeric enzymes were designed by rational exchange of cap and C-terminal flap, between CduLAc and CalLAc8. The results show that the cap region plays a significant role in substrate specificity; the main core was found to be the most important part of the protein for acyltransfer ability. Similar exchanges were made with CAL-A from Candida antarctica, but only the C-terminal exchange was successful. Yet, the role of this domain was not clearly elucidated, other than that it is essential for activity.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)


What can I do for you?
Get Best Price

Get Best Price for 10024-47-2