82499-20-5

Usage

Uses

Used in Food Industry:
(1R)-1-hydroxy-1-(3-hydroxyphenyl)propan-2-one is used as a flavoring agent for its fruity aroma and flavor, commonly found in various fruits such as raspberries, cranberries, and blackberries.
Used in Cosmetic Industry:
(1R)-1-hydroxy-1-(3-hydroxyphenyl)propan-2-one is used as a fragrance ingredient for its fruity aroma, enhancing the scent of cosmetic products.
Used in Weight Loss Supplements:
(1R)-1-hydroxy-1-(3-hydroxyphenyl)propan-2-one is used as a weight loss supplement due to its potential to increase the breakdown of fat and boost metabolism.
Used in Antioxidant and Anti-Inflammatory Applications:
(1R)-1-hydroxy-1-(3-hydroxyphenyl)propan-2-one is being studied for its potential antioxidant and anti-inflammatory properties, which may have beneficial effects on human health.
Used in Skin Care Products:
(1R)-1-hydroxy-1-(3-hydroxyphenyl)propan-2-one is being studied for its potential to improve skin elasticity and reduce signs of aging, making it a promising ingredient for skin care products.
However, further research is needed to fully understand the effects of (1R)-1-hydroxy-1-(3-hydroxyphenyl)propan-2-one on human health and its safety for long-term use.

Upstream product

• 57-60-3 piruvate 
• 100-83-4 meta-hydroxybenzaldehyde 
• 127-17-3 2-oxo-propionic acid 

Downstream Products

• 54-49-9 (1R,2S)-metaraminol 

Relevant academic research and scientific papers

Structural and Mutagenesis Studies of the Thiamine-Dependent, Ketone-Accepting YerE from Pseudomonas protegens

A wide range of thiamine diphosphate (ThDP)-dependent enzymes catalyze the benzoin-type carboligation of pyruvate with aldehydes. A few ThDP-dependent enzymes, such as YerE from Yersinia pseudotuberculosis (YpYerE), are known to accept ketones as acceptor substrates. Catalysis by YpYerE gives access to chiral tertiary alcohols, a group of products difficult to obtain in an enantioenriched form by other means. Hence, knowledge of the three-dimensional structure of the enzyme is crucial to identify structure–activity relationships. However, YpYerE has yet to be crystallized, despite several attempts. Herein, we show that a homologue of YpYerE, namely, PpYerE from Pseudomonas protegens (59 % amino acid identity), displays similar catalytic activity: benzaldehyde and its derivatives as well as ketones are converted into chiral 2-hydroxy ketones by using pyruvate as a donor. To enable comparison of aldehyde- and ketone-accepting enzymes and to guide site-directed mutagenesis studies, PpYerE was crystallized and its structure was determined to a resolution of 1.55 ?.

Asymmetric synthesis of (: S)-phenylacetylcarbinol-closing a gap in C-C bond formation

(S)-Phenylacetylcarbinol [(S)-PAC] and its derivatives are valuable intermediates for the synthesis of various active pharmaceutical ingredients (APIs), but their selective synthesis is challenging. As no highly selective enzymes or chemical catalysts were available, we used semi-rational enzyme engineering to tailor a potent biocatalyst to be >97% stereoselective for the synthesis of (S)-PAC. By optimizing the reaction and process used, industrially relevant product concentrations of >48 g L-1 (up to 320 mM) were achieved. In addition, the best enzyme variant gave access to a broad range of ring-substituted (S)-PAC derivatives with high stereoselectivity, especially for meta-substituted products.