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2361-97-9

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2361-97-9 Usage

Description

L-Phenylalanine, N-acetyl-, propyl ester is a chemical compound derived from the amino acid phenylalanine, featuring an acetyl group and a propyl ester. It is recognized for its potential to support neurological health and cognitive function, as well as for its antioxidant properties that may protect the brain from oxidative stress and age-related cognitive decline.

Uses

Used in Neurological Health Supplements:
L-Phenylalanine, N-acetyl-, propyl ester is used as a cognitive enhancer for its ability to support the production of neurotransmitters such as dopamine, norepinephrine, and epinephrine. It is believed to have benefits for mood enhancement, memory and learning, and overall cognitive performance.
Used in Nootropic Formulas:
As a component of nootropic formulas, L-Phenylalanine, N-acetyl-, propyl ester is utilized for its potential to improve cognitive function and support brain health.
Used in Skincare Products:
L-Phenylalanine, N-acetyl-, propyl ester is used in skincare applications for its potential anti-aging and skin brightening effects, capitalizing on its antioxidant properties to protect the skin from oxidative stress and promote a youthful appearance.
Used in Antioxidant Therapies:
L-Phenylalanine, N-acetyl-, propyl ester is also considered for use in antioxidant therapies aimed at reducing oxidative stress in the brain, which may help in preventing or mitigating age-related cognitive decline.

Check Digit Verification of cas no

The CAS Registry Mumber 2361-97-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,3,6 and 1 respectively; the second part has 2 digits, 9 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 2361-97:
(6*2)+(5*3)+(4*6)+(3*1)+(2*9)+(1*7)=79
79 % 10 = 9
So 2361-97-9 is a valid CAS Registry Number.

2361-97-9Downstream Products

2361-97-9Relevant articles and documents

Ionic-surfactant-coated subtilisin: Activity, enantioselectivity, and application to dynamic kinetic resolution of secondary alcohols

Kim, Kyungwoo,Lee, Eungyeong,Kim, Cheolwoo,Park, Jaiwook,Kim, Mahn-Joo

, p. 8836 - 8844 (2017/11/03)

In this work, we explored the utility of ionic-surfactant-coated Bacillus licheniformis subtilisin (ISCBLS) as the catalyst for the dynamic kinetic resolution of secondary alcohols. ISCBLS was prepared by freeze-drying Bacillus licheniformis subtilisin wi

Urea treated subtilisin as a biocatalyst for transformations in organic solvents

Mukherjee, Joyeeta,Mishra, Prasant,Gupta, Munishwar N.

, p. 1976 - 1981 (2015/03/30)

Abstract Subtilisin lyophilized from its solution in aqueous buffer in the presence of 6 M urea showed up to 50-fold increase (as compared to lyophilized subtilisin not subjected to urea treatment) in its initial rate of a transesterification reaction in anhydrous n-hexane. The lyophilization time controlling the extent of 'drying' was an important parameter. The urea treated subtilisin had five times shorter half life during heating at 100 C in hexane. The change in conformation was also reflected in its 92-fold higher activity at 15 C as compared to merely 28-fold higher activity at 45 C. The comparative enantioselectivity of urea treated subtilisin during kinetic resolution of 1-phenylethanol was expectedly lower. Its enantioselectivity during kinetic resolution of a natural substrate N-acetyl-(R,S)-phenylalanine ethyl ester in hexane was higher. Urea treated subtilisin also showed higher catalytic promiscuity during an aldol condensation. CD studies in both far UV and near UV region were also carried out to compare the two structures.

Protease activation in glycerol-based deep eutectic solvents

Zhao, Hua,Baker, Gary A.,Holmes, Shaletha

experimental part, p. 163 - 167 (2012/07/01)

Deep eutectic solvents (DESs) consisting of mixtures of a choline salt (chloride or acetate form) and glycerol are prepared as easily accessible, biodegradable, and inexpensive alternatives to conventional aprotic cation-anion paired ionic liquids. These DES systems display excellent fluidity coupled with thermal stability to nearly 200 °C. In this work, the transesterification activities of cross-linked proteases (subtilisin and α-chymotrypsin), immobilized on chitosan, were individually examined in these novel DESs. In the 1:2 molar ratio mixture of choline chloride/glycerol containing 3% (v/v) water, cross-linked subtilisin exhibited an excellent activity (2.9 μmol min -1 g-1) in conjunction with a selectivity of 98% in the transesterification reaction of N-acetyl-l-phenylalanine ethyl ester with 1-propanol. These highly encouraging results advocate more extensive exploration of DESs in protease-mediated biotransformations of additional polar substrates and use of DESs in biocatalysis more generally.

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