메뉴 건너뛰기




Volumn 45, Issue 36, 2004, Pages 6713-6716

Lipase-catalyzed kinetic resolution of α-hydroxy-H-phosphinates

Author keywords

Kinetic resolution; Lipase; Phosphinic acids and derivatives

Indexed keywords

ACETIC ACID; PHOSPHORUS DERIVATIVE; TRIACYLGLYCEROL LIPASE;

EID: 4344716612     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tetlet.2004.07.066     Document Type: Article
Times cited : (28)

References (29)
  • 21
    • 4344615681 scopus 로고    scopus 로고
    • note
    • P*)-3a might be associated with partial hydrolysis of their phosphinate moiety in the reaction mixture
  • 22
    • 4344655679 scopus 로고    scopus 로고
    • note
    • P)-3a might be associated with both loss at the purification step and partial hydrolysis of their phosphinate moiety in the reaction mixture
  • 23
    • 4344676586 scopus 로고    scopus 로고
    • note
    • +): 279.0762; found: 279.0773
  • 24
    • 4344663569 scopus 로고    scopus 로고
    • note
    • We also examined reactions of 3b with other enzymes such as lipase AY-30 (Candida rugosa), lipase AS (Aspergillus nieger), lipase F-AP 15 (Rhizopus oryzae). While the desired reaction did not proceed in the presence of lipase AY-30, employing lipase AS gave the hydrolysis product (36% yield) as a mixture of diastereomers (1:2.1). The reaction in the presence of lipase F-AP 15 provided the product as a diastereomixture (1:2.4) in low yield (5%). Thus, lipase PS proved to be the optimum enzyme among those examined for resolving α-hydroxy-H-phosphinates


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.