Lipase-enhanced activity in flavour ester reactions by trapping enzyme conformers in the presence of interfaces

✍ Scribed by Herminia González-Navarro; Lorenzo Braco

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 100 KB
• Volume: 59
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(19980705)59:1<122::aid-bit16>3.0.co;2-k

✦ Synopsis

In order to improve the lipase-catalyzed synthesis of flavour esters, we have used the reported strategy of interfacial activation-based molecular (bio)imprinting [Mingarro et al. 1995. Proc. Natl. Acad. Sci. U.S.A. 92: 3308], later called trapping in the presence of amphiphile interfaces (TPI) [Mingarro et al. 1996. Biochemistry 35: 9935]. Five lipases of fungal and mammalian origin typically used for esterification process have been explored to improve production by TPI treatment. A marked enhancement of enzymatic activity has been observed in all TPI-treated lipases assayed and the activation factor obtained was up to 90-fold. The dependence on chain length of acyl donors in the esterification of geranyl alcohol has been investigated, showing clear differences between activated and nonactivated lipase. The results indicate that this rational approach leads to conversion yields that are remarkably higher, not only than its counterpart pH-optimized control lipase, but also the ''protected'' lipase by conventional methods (lyoprotectans or salts). We propose this strategy as a promising tool to be used in more industrial biotransformations.