Advantages in using immobilized thermophilic β-glycosidase in nonisothermal bioreactors

✍ Scribed by F. Febbraio; M. Portaccio; S. Stellato; S. Rossi; U. Bencivenga; R. Nucci; M. Rossi; F. S. Gaeta; D. G. Mita

• Book ID: 101241058
• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 290 KB
• Volume: 59
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(19980705)59:1<108::aid-bit14>3.0.co;2-e

✦ Synopsis

Catalytic membranes, obtained by immobilizing thermophilic ␤-glycosidase onto nylon supports, were used in a nonisothermal bioreactor to study the effect of temperature gradients on the rate of enzyme reaction. Two experimental approaches were carried out to explain the molecular mechanisms by which the temperature gradients affect enzyme activity. The results showed that the thermophilic enzyme behaved as the mesophilic ␤-galactosidase, exhibiting an activity increase which was linearly proportional to the transmembrane temperature difference. The efficiency of the system proposed was determined by calculating two constants, ␣ and ␤, which represent respectively the percentage increase of enzyme activity when a temperature difference of 1°C or a temperature gradient of 1°C cm -1 were applied across the catalytic membrane. The increase of enzyme activity in nonisothermal bioreactors entailed a proportional reduction of production times. The advantages in using thermophilic enzymes immobilized in nonisothermal bioreactors are also discussed.