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Control of recombinant human endostatin production in fed-batch cultures of Pichia pastoris using the methanol feeding rate

Control of recombinant human endostatin production in fed-batch cultures of Pichia pastoris using... Endostatin is a 20 kDa carboxyl-terminal fragment of collagen XVIII that strongly inhibits angiogenesis and tumor growth. The methylotrophic yeast, Pichia pastoris, is a robust expression system that can be used to study methods to improve the yields of rhEndostatin. We expressed rhEndostatin in P. pastoris under the control of the alcohol oxidase 1 (aox 1) promoter (Mut+ phenotype) as a model, and used a cell biomass of about 50 g l−1 dry cell wt as a starting point for the induction phase and varied the methanol feed rate at 8 ml l−1 h−1, 11 ml l−1 h−1 and 15 ml l−1 h−1. While the cell growth rate was proportional to the rate of methanol delivery, protein production rate was not. These findings could be used to guide parameters for large-scale production of recombinant proteins in the P. pastoris system. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Letters Springer Journals

Control of recombinant human endostatin production in fed-batch cultures of Pichia pastoris using the methanol feeding rate

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References (17)

Publisher
Springer Journals
Copyright
Copyright © 2002 by Kluwer Academic Publishers
Subject
Life Sciences; Biotechnology; Organic Chemistry; Biochemistry, general; Microbiology; Animal Anatomy / Morphology / Histology
ISSN
0141-5492
eISSN
1573-6776
DOI
10.1023/A:1020357732474
Publisher site
See Article on Publisher Site

Abstract

Endostatin is a 20 kDa carboxyl-terminal fragment of collagen XVIII that strongly inhibits angiogenesis and tumor growth. The methylotrophic yeast, Pichia pastoris, is a robust expression system that can be used to study methods to improve the yields of rhEndostatin. We expressed rhEndostatin in P. pastoris under the control of the alcohol oxidase 1 (aox 1) promoter (Mut+ phenotype) as a model, and used a cell biomass of about 50 g l−1 dry cell wt as a starting point for the induction phase and varied the methanol feed rate at 8 ml l−1 h−1, 11 ml l−1 h−1 and 15 ml l−1 h−1. While the cell growth rate was proportional to the rate of methanol delivery, protein production rate was not. These findings could be used to guide parameters for large-scale production of recombinant proteins in the P. pastoris system.

Journal

Biotechnology Letters – Springer Journals

Published: Oct 10, 2004

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