An experimental analysis of membrane bioreactor performances with immobilized chymosin

Citation
S. Curcio et al., An experimental analysis of membrane bioreactor performances with immobilized chymosin, J MEMBR SCI, 173(2), 2000, pp. 247-261
Citations number
22
Categorie Soggetti
Chemistry,"Chemical Engineering
Journal title
JOURNAL OF MEMBRANE SCIENCE
ISSN journal
03767388 → ACNP
Volume
173
Issue
2
Year of publication
2000
Pages
247 - 261
Database
ISI
SICI code
0376-7388(20000715)173:2<247:AEAOMB>2.0.ZU;2-R
Abstract
Aim of the present work is the experimental analysis of a continuos flow me mbrane bioreactor with immobilized chymosin for the hydrolysis of milk k-ca sein, one of the steps in the cheese production process. Chymosin has been immobilized on the bioreactor membrane by ultrafiltering under pressure its solutions, continuously fed to the system in a total recycle configuration . Bioreactor performances are evaluated in terms of two different parameter s: chymosin activity and its release. The former, indirectly, measures the amount of k-casein converted into reaction products (para-k-casein and Glyc oMacroPeptide, GMP); the latter quantifies the amount of biocatalyst that i s removed from the membrane by the milk flowing stream. A theoretical approach, based on the boundary layer theory, has also been a ttempted to estimate the dependence of chymosin release upon the wall shear stress and on the back-diffusion phenomena towards the milk bulk. The expe rimental analysis of bioreactor behavior has been carried out, searching fo r the operating conditions and system configurations that maximized chymosi n activity and minimized its release. Particular attention has been devoted to the selection of the membrane material: PolySulphone membranes offered the best performance during experiments, as compared to those of PolyPropil ene and PolyVinilDeneFluoride. The system configuration that gave best resu lts, both in terms of enzyme activity and of its release, was based on a co ntinuous milk recycle to the bioreactor. Enzyme losses were confined to 5-1 0 mg/l range, whereas its activity always attained values high enough (>2 g /l) to promote the coagulation in the next heating step of destabilized mil k. During the experiments, an optimal value of the recycle ratio, was also found. (C) 2000 Elsevier Science B.V. All rights reserved.