for loadings higher than 10% in AlPO4-Sepiolite. FFA content increased with lipase load. Thermal oxidation was negligible. For all the biocatalysts tested, the catalytic activity increased with the aw. A 100% SFC35 • C reduction was observed after six hours of reaction, at aw of 1. However, the esti
✦ LIBER ✦
Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants
✍ Scribed by Marina Guillén; Maria Dolors Benaiges; Francisco Valero
- Publisher
- American Institute of Chemical Engineers
- Year
- 2011
- Tongue
- English
- Weight
- 764 KB
- Volume
- 27
- Category
- Article
- ISSN
- 8756-7938
- DOI
- 10.1002/btpr.654
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## Abstract A continuous fermentation process has been developed in __Pichia pastoris (P. pastoris__) with the glyceraldehyde‐3‐phosphate dehydrogenase (__GAP__) promoter in order to produce large quantities of recombinant human chitinase (rh‐chitinase) for preclinical studies as a potential high‐d