## Abstract The demand for recombinant proteins for medical and industrial use is expanding rapidly and plants are now recognized as an efficient, inexpensive means of production. Although the accumulation of recombinant proteins in transgenic plants can be low, we have previously demonstrated that
Expression of a recombinant elastin-like protein in pichia pastoris
โ Scribed by Rory E. Sallach; Vincent P. Conticello; Elliot L. Chaikof
- Publisher
- American Institute of Chemical Engineers
- Year
- 2009
- Tongue
- English
- Weight
- 211 KB
- Volume
- 25
- Category
- Article
- ISSN
- 8756-7938
- DOI
- 10.1002/btpr.208
No coin nor oath required. For personal study only.
โฆ Synopsis
Abstract
The translation of highly repetitive gene sequences is often associated with reduced levels of protein expression and may be prone to mutational events. In this report, we describe a modified concatemerization strategy to construct a gene with enhanced sequence diversity that encodes a highly repetitive elastinโlike protein polymer for expression in Pichia pastoris. Specifically, degenerate oligonucleotides were used to create a monomer library, which after concatemerization yielded a genetically nonrepetitive DNA sequence that encoded identical pentapeptide repeat sequences. By limiting genetic repetition, the risk of genetic deletions, rearrangements, or premature termination errors during protein synthesis is minimized. ยฉ 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009
๐ SIMILAR VOLUMES
The use of the methylotrophic yeast, Pichia pastoris, as a cellular host for the expression of recombinant proteins has become increasing popular in recent times. P. pastoris is easier to genetically manipulate and culture than mammalian cells and can be grown to high cell densities. Equally importa
## Abstract A continuous fermentation process has been developed in __Pichia pastoris (P. pastoris__) with the glyceraldehydeโ3โphosphate dehydrogenase (__GAP__) promoter in order to produce large quantities of recombinant human chitinase (rhโchitinase) for preclinical studies as a potential highโd