ISSN:
1573-6784
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract Two single-step purification methods were used to isolate the recombinant protein, rBm86, produced in Pichia pastoris. Salting-out results in a compromise between final purity and recovery of rBm86. At 15, 25 and 35% of ammonium sulphate saturation (pH 7), rBm86 concentration in the supernatant phase was proportional to the initial amount of protein. Acid precipitation of contaminants resulted in 98% purity and 98% recovery of rBm86. High aggregation of rBm86, forming particles of 28 nm, changed the isoelectric point of monomers (5.5), considering only the aminoacid sequence, to 4.5 for particles.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1018438805811
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