Advertisement

Bioprocess Engineering

, Volume 13, Issue 4, pp 205–210 | Cite as

Modelling and analysis of the continuous affinity-recycle extraction process: a case of specific elution with low molecular weight competitive inhibitor

  • Y. Sun
  • J. -L. Xue
  • X. -Y. Dong
Originals

Abstract

The continuous affinity-recycle extraction (CARE) process of specifie elution with low molecular weight competitive inhibitor is mathematically modelled taking into account the presence of membrane rejections to the components in a crude broth. The process performance, defined as purification factor (PF) and recovery yield (REC), is analyzed by computer simulations. The results show that for constant affinity systems (ligate and ligand as well as inhibitor) and operating conditions an optimal value of the inhibitor concentration exists to give maxima of REC and PF, and the optimal value decreases with the increase of the affinity binding constant of ligate and inhibitor. Although the increase in affinity-recycle flow rate results in the decrease of PF, an optimal value of the affinity-recycle flow rate exists to show a maximum of REC. Hence in the process design the selection of the affinity-recycle flow rate is also of importance to obtain higher REC and PF simultaneously. The consideration of membrane rejections will in practice be useful to analyse the separation of a binary broth using ultrafiltration membranes which reject to the components. For a multicomponent broth, however, membranes without rejection to all components should be employed to simplify the process design and optimization. In general, the model is useful to design a CARE process using nonporous microparticles or macromolecules as affinity supports.

Keywords

Waste Water Water Pollution Macromolecule Affinity Binding Process Design 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

List of Symbols

Ci mol/l

contaminant concentration in feed

C01 mol/l

contaminant concentration in waste stream

C02 mol/l

contaminant concentration in product stream

ei mol/l

ligate concentration in feed

ej mol/l

free ligate concentration in Con. j

Elj mol/l

concentration of ligate bound to ligand in Con.

Eoj mol/l

ligate concentration in waste (j=1) or product (j=2) stream

Etj mol/l

total ligate concentration in Con. j

Exj mol/l

concentration of ligate bound to inhibitor in Con. j

Fe l/s

eluant flow rate

Fi l/s

feed flow rate

Foj l/s

flow rate of waste (j=1) or product (j=2) stream

Fr l/s

affinity-recycle flow rate

fj

affinity binding fraction of ligate to ligand in Con.

j

index for container No., j=1 for Con. 1 and j=2 for Con. 2

kl l/mol

affinity binding constant of ligate and ligand

Kx l/mol

affinity binding constant of ligate and inhibitor

Lo mol/l

total ligand concentration in both containers

Lj mol/l

free ligand concentration in Con. j

PF

purification factor

REC%

recovery yield

Rj

rejection coefficient of total ligate in Con. j

Rm

membrane rejection coefficient of free ligate

Rmc

membrane rejection coefficient of contaminant

re

ratio of eluant to feed flow rate

rr

ratio of affinity-recycle to feed flow rate

Xoj mol/l

inhibitor concentration in waste (j=1) or product (j=2) stream

Xej mol/l

concentration of inhibitor bound to ligate in Con. j

Xi mol/1

inhibitor concentration in eluant feed

Xj mol/l

free inhibitor concentration in Con. j

Xtj mol/l

total inhibitor concentration in Con. j

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Mattiasson, B.; Ramstorp, M.: Ultrafiltration affinity purification: Isolation of concanavalin A from seeds of Canavalia ensiformis. J. Chromatogr. 283 (1984) 323–330CrossRefGoogle Scholar
  2. 2.
    Pungor, E. Jr.; Afeyan, N. B.; Gordon, N. F.: Continuous affinity-recycle extraction: a novel protein separation technique. Bio/technol. 5 (1987) 604–608CrossRefGoogle Scholar
  3. 3.
    Luong, J. H. T.; Male, K. B.; Nguyen, A. L.: Synthesis and characterization of a water-soluble affinity polymer for trypsin purification. Biotechnol. Bioeng. 31 (1988) 439–446Google Scholar
  4. 4.
    Power, D. J.; Kilpatrick, P. K.; Carbonell, R. G.: Trypsin purification by affinity binding to small unilamellar liposomes. Biotechnol. Bioeng. 36 (1990) 506–519Google Scholar
  5. 5.
    Luong, J. H. T.; Male, K. B.; Nguyen, A. L.: A continuous affinity ultrafiltration process for trypsin purification. Biotechnol. Bioeng. 31 (1988) 516–520Google Scholar
  6. 6.
    Luong, J. H. T.; Male, K. B.; Nguyen, A. L.: Mathematical modeling of affinity ultrafiltration process. Biotechnol. Bioeng. 32 (1988) 451–459Google Scholar
  7. 7.
    Afeyan, N. B.; Gordon, N. F.; Cooney, C. L.: Mathematical modeling of the continuous affinity-recycle extraction purification technique. J. Chromatogr. 478 (1989) 1–19CrossRefGoogle Scholar
  8. 8.
    Sun, Y.; Yu, K.; Zhou, X.-Z.: Polymerized liposome as an affinity support for enzyme affinity ultrafiltration. In: Teo, W.; Yap, M.; Oh, S. (Ed.): Better Living Through Innovative Biochem. Eng. pp. 613–615. Singapore: Continental Press 1994Google Scholar
  9. 9.
    Weiner, C.; Sara, M.; Dasgupta, G.; Sleytr, U. B.: Affinity cross-flow filtration: purification of IgG with a novel protein A affinity matrix prepared from two-dimensional protein crystals. Biotechnol. Bioeng. 44 (1994) 55–65Google Scholar

Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • Y. Sun
    • 1
  • J. -L. Xue
    • 1
  • X. -Y. Dong
    • 1
  1. 1.Department of Chemical Engineering and Biotechnology CenterTianjin UniversityTianjinP. R. China

Personalised recommendations