Polyethylene glycol-modified lipase catalyzes asymmetric alcoholysis of ?-decalactone in n-decanol
| Autor: | Makoto Furukawa, Takeshi Uemura, Katsukiyo Sakurai, Yuji Inada, Yoh Kodera, Hideyuki Kuno, Hajime Matsushita, Ayako Matsushima, Misao Hiroto |
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| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Triacylglycerol lipase Chemical modification Bioengineering General Medicine Polyethylene glycol Applied Microbiology and Biotechnology chemistry.chemical_compound biology.protein Organic chemistry Lipase Enantiomeric excess Ethylene glycol Lactone Alkyl Biotechnology |
| Zdroj: | Biotechnology Letters. 17:61-66 |
| ISSN: | 1573-6776 0141-5492 |
| Popis: | Lipase from Pseudomonas cepacia was modified with 2,4-bis[O-methoxypoly(ethylene glycol)]-6-chloro-s-triazine(activated PEG2) to form PEG-lipase. The PEG-lipase, soluble and active in organic solvents, catalyzes asymmetric alcoholysis of racemic δ-decalactone in alcohols to form (R)-5-hydroxydecanoic acid alkyl esters. The yield was 69% with 83% enantiomeric excess after 3 hr-reaction in n-decanol at 50°C. The advantage of this reaction is that the alcoholysis proceeds efficiently in straight hydrophobic substrates without any organic solvents. |
| Databáze: | OpenAIRE |
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