107832-33-7

Usage

Uses

Used in the Fragrance Industry:
(R)-(1-PHENYLETHYL)SUCCINATE is used as a key ingredient in the production of perfumes and fragrances, leveraging its distinctive fruity and floral scent to enhance the overall aroma of various products.
Used in the Flavor Industry:
In the food industry, (R)-(1-PHENYLETHYL)SUCCINATE serves as a flavoring agent, adding a pleasant taste to different types of food products, capitalizing on its unique flavor profile.
Used in the Pharmaceutical Industry:
(R)-(1-PHENYLETHYL)SUCCINATE is present in some natural sources and is being studied for its potential biological and pharmacological activities, indicating its possible use in the development of new drugs and therapies.

Upstream product

• 108-30-5 succinic acid anhydride 
• 98-85-1 1-Phenylethanol 
• 76620-61-6 (±)-3-((1-phenylethoxy)carbonyl)propanoic acid 

Downstream Products

• 1517-69-7 (R)-1-phenylethanol 

Relevant academic research and scientific papers

CONVENIENT PRACTICAL RESOLUTION OF RACEMIC ALKYL-ARYL ALCOHOLS VIA ENZYMATIC ACYLATION WITH SUCCINIC ANHYDRIDE IN ORGANIC SOLVENTS

Enantiomerically pure alkyl-aryl secondary alcohols were conveniently obtained on a kilogram scale from their racemic mixtures by enzymatic acylation with succinic anhydride in organic solvents.A major advantage of this acylation method is the ease of separating the ester from the unreacted alcohol.This is achieved by extracting the organic solution with aqueous NaHCO3 after the enzymatic reaction is completed.

Enzymatic kinetic resolution of sec-alcohols using an ionic liquid anhydride as acylating agent

A task-specific ionic liquid bearing an anhydride moiety was synthesized for the first time in good yield (83%) through a carbodiimide-mediated coupling reaction. The enantiomeric separation of a series of sec-alcohols was performed via enzymatic kinetic resolution, employing an ionic anhydride as acylating agent and Candida antarctica Lipase B as a biocatalyst. A fast and efficient recovery of both enantiomers was achieved separately due to the ionic nature of the acyl donor, combined with the possibility of carrying out the enzymatic step in an organic solvent.

Enantioselective esterase activity of an industrial glutaryl acylase

The unexpected esterase activity of an industrial glutaryl acylase was investigated. Glutaryl esters of a series of primary and secondary alcohols as well as of phenols were all efficiently hydrolyzed, the only exception being the sterically hindered glutarate of thymol. The enantioselectivities of the acylase, which were evaluated with three of these substrates, were quite low (E values ranging between 1.9 and 7.2), but were significantly improved by substrate and/or solvent engineering. Enantiomerically enriched hydrolyzed alcohols and unreacted glutarates can be easily separated by selective extraction, thus avoiding chromatographic steps.