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How large are the active sites of the lipases from Candida rugosa and from Pseudomonas cepacia ?

✍ Scribed by Christina Exl; Helmut Hönig; Gerald Renner; Renate Rogi-Kohlenprath; Veronika Seebauer; Peter Seufer-Wasserthal

Book ID
103976905
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
380 KB
Volume
3
Category
Article
ISSN
0957-4166

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✦ Synopsis

Racemates of 2-Azido alcohols of large, polycyclic systems can be resolved by enzyme catalyzed hydrolysis of the respective butyrates using lipases from Candida rugosa (cylincfracea) and from Pseudomonas cepacia (ffuomscens) with excellent optiwl and chemical yiefds. An estimate of the size of the respective hydrophobic pockets of these lipases is given.

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Influence of the nature of modifier in t
Influence of the nature of modifier in the enzymatic activity of chemical modified semipurified lipase from Candida rugosa
✍ M. J. Hernáiz; J. M. Sánchez-Montero; J. V. Sinisterra 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 196 KB 👁 2 views

Semipurified lipase of Candida rugosa (CRSL) was subjected to chemical modification, and the activities of the modified lipase, in hydrolysis and esterification reactions, were examined. The esterification reactions were carried out in the absence and presence of isooctane. When the enzyme was modif