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Recovery of recombinant beta-glucosidase by expanded bed adsorption from Pichia pastoris high-cell-density culture broth
KTH, School of Biotechnology (BIO).
KTH, School of Biotechnology (BIO).
KTH, School of Biotechnology (BIO), Bioprocess Technology.
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2006 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 122, no 1, 86-98 p.Article in journal (Refereed) Published
Abstract [en]

Methanol limited fed-batch cultivation was applied for production of a plant derived beta-glucosidase by Pichia pastoris. The beta-glucosidase was recovered by expanded bed adsorption chromatography applied to the whole culture broth. The new Streamline Direct HST1 adsorbent was compared with Streamline SP. Higher bead density made it possible to operate at two times higher feedstock concentration and at two times higher flow velocity. The higher binding capacity in the conductivity range 0-48 mS cm(-1) of Streamline Direct HST1 might be caused by the more complex interaction of multi-modal ligand in Streamline Direct HST1 compared to the single sulphonyl group in Streamline SP. Harsher elution condition had to be applied for dissociation of beta-glucosidase from Streamline Direct HST1 due to stronger binding interaction. The 5% dynamic binding capacity was 160 times higher for Streamline Direct HST1 compared to Streamline SP. The yield of beta-glucosidase on Streamline Direct HST 1 (74%) was significantly higher than on Streamline SP (48%). Furthermore, beta-glucosidase was purified with a factor of 4.1 and concentrated with a factor of 17 on Streamline Direct HST1 while corresponding parameters were half of these values for Streamline SP. Thus, for all investigated parameters Streamline Direct HST1 was a more suitable adsorbent for recovery of recombinant beta-glucosidase from unclarified P. pastoris high-cell-density cultivation broth.

Place, publisher, year, edition, pages
2006. Vol. 122, no 1, 86-98 p.
Keyword [en]
beta-glucosidase, Pichia pastoris, methanol limited fed-batch, expanded bed adsorption, multi-modal ligand, methylotrophic yeast, protein-purification, chromatography, expression, binding
National Category
Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-15530DOI: 10.1016/j.jbiotec.2005.08.016ISI: 000236102300009Scopus ID: 2-s2.0-32644473166OAI: oai:DiVA.org:kth-15530DiVA: diva2:333571
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved
In thesis
1. Process design for production of Thai rosewood β-glucosidase in Pichia pastoris
Open this publication in new window or tab >>Process design for production of Thai rosewood β-glucosidase in Pichia pastoris
2005 (English)Licentiate thesis, comprehensive summary (Other scientific)
Place, publisher, year, edition, pages
Stockholm: KTH, 2005. 50 p.
National Category
Industrial Biotechnology
Identifiers
urn:nbn:se:kth:diva-375 (URN)91-7178-081-5 (ISBN)
Presentation
2005-06-10, FB54, AlbaNova, Roslagstullsbacken 21, Stockholm, 11:00
Supervisors
Note
QC 20101126Available from: 2005-08-08 Created: 2005-08-08 Last updated: 2010-11-26Bibliographically approved

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