Journal
BIORESOURCE TECHNOLOGY
Volume 101, Issue 4, Pages 1318-1323Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2009.09.025
Keywords
Pichia pastoris; Polygalacturonate lyase (PGL); Sorbitol; Proteolytic degradation; Alcohol oxidase
Funding
- National Outstanding Youth Foundation of China [20625619]
- Key Project of Chinese National Programs for Fundamental Research and Development (973 program) [2007CB714306, 20070714303]
- Program for New Century Excellent Talents in University [NCET-07-0378]
- National Natural Science Foundation of China [20836003]
- Key Technologies R & D Program of Jiangsu Province, China [SBE200900022]
- Innovative Research Team in University, Jiangsu Province, China
- National High Technology Research and Development Program of China [2009AA02Z204]
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Alkaline polygalacturonate lyase (PGL) production by Pichia pastoris GS115 was used as a model to study the mechanism and strategy for enhancing heterologous protein production. In order to enhance cell viability and volumetric recombinant protein productivity, sorbitol, which had been confirmed to be a non-repressive carbon source, was added together with methanol during the induction phase. The resultant PGL activity was up to 1593 U mL(-1), which was enhanced 1.85-fold compared to the control (863 U mL-1) cultured with sorbitol added at a constant rate of 3.6 g h(-1) L-1 after an induction period of 100 h. Further results revealed that an appropriate sorbitol co-feeding strategy not only decreased the cell mortality to 8.8% (the control is about 23.1%) in the end of fermentation, but also reduced the proteolytic degradation of PGL. (C) 2009 Elsevier Ltd. All rights reserved.
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