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Titolo:
Substrate specificity of lipase B from Candida antarctica in the synthesisof arylaliphatic glycolipids
Autore:
Otto, RT; Scheib, H; Bornscheuer, UT; Pleiss, J; Syldatk, C; Schmid, RD;
Indirizzi:
Univ Stuttgart, Inst Tech Biochem, D-70569 Stuttgart, Germany Univ Stuttgart Stuttgart Germany D-70569 hem, D-70569 Stuttgart, Germany Univ Stuttgart, Inst Bioverfahrenstechn, D-70569 Stuttgart, Germany Univ Stuttgart Stuttgart Germany D-70569 chn, D-70569 Stuttgart, Germany
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 4-6, volume: 8, anno: 2000,
pagine: 201 - 211
SICI:
1381-1177(20000218)8:4-6<201:SSOLBF>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHIZOPUS-ORYZAE LIPASE; N-ALKYL-GLUCOSIDE; IMMOBILIZED LIPASE; CRYSTAL-STRUCTURE; SERINE PROTEASE; BINDING-SITES; ACIDS; ESTERIFICATION; ESTERS; INHIBITION;
Keywords:
Candida antarctica lipase B; aromatic glycolipids; salicin; computer-aided molecular modeling;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Schmid, RD Univ Stuttgart, Inst Tech Biochem, Allmandring 31, D-70569 Stuttgart, Germany Univ Stuttgart Allmandring 31 Stuttgart Germany D-70569 ermany
Citazione:
R.T. Otto et al., "Substrate specificity of lipase B from Candida antarctica in the synthesisof arylaliphatic glycolipids", J MOL CAT B, 8(4-6), 2000, pp. 201-211

Abstract

Arylaliphatic glycolipids are known for their pharmaceutical and medicinalproperties. We found that a great variety of arylaliphatic esters can be synthesized from non-activated substrates like glucose or the natural occurring drug salicin using lipase B from Candida antarctica (CAL-B). However, esters based on aromatic carboxylic acids or unsaturated arylaliphatic acids, like cinnamic acid and its derivatives, which are known to display anticancer activity, could not be obtained. In this work, we performed computer-aided molecular modeling based on data of our work published recently and syntheses of new glycolipids to understand why some substances are accepted by CAL-B while some are not. For this purpose, we investigated the accessibility of the lipase binding site for the arylaliphatic acyl donors as well as the steric interactions between the aglycons of glucosides and the residues of the alcohol binding pocket in order to elucidate potentials and limitations of CAL-B for the synthesis of aromatic glycolipids. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 18:30:53