Adsorptive control of water in esterification with immobilized enzymes: I. Batch reactor behavior

✍ Scribed by Paul Mensah; John L. Gainer; Giorgio Carta

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 246 KB
• Volume: 60
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(19981120)60:4<434::aid-bit5>3.0.co;2-n

✦ Synopsis

Reducing the influence of an undesired product in an enzymatic reaction could have a significant impact on the productivity of such systems. Here, we focus on the removal of water formed during an enzymatic esterification in a batch reactor. A commercial immobilized lipase preparation, known as Lipozyme, is used as the biocatalyst and propionic acid and isoamyl alcohol dissolved in hexane are the substrates. In this system, the water formed will partition between the catalyst and the medium. As the more polar reactants are converted into the less polar ester product, the water is partitioned more towards the biocatalyst and the accumulation of water eventually causes lower reaction rates. Addition of a strong-acid cation exchange resin in sodium form is found to control the water accumulation on the biocatalyst without stripping the essential water needed for the enzyme to function and substantial improvements in conversion are achieved. A mathematical model is developed to describe the batch reaction behavior with and without added absorbent, which successfully predicts the behavior of water and its effects.