A rapid and convenient method for graduation, isolation, and purification of laccase from Trametes versicolor and Fomes fomentarius culture fluids was developed. For purification affinity chromatography on syringyl-and vanillylcontrolled porosity glass (CPG) columns was applied. The purified laccase
Stepwise elution chromatography as a method for both purification and concentration of proteins
β Scribed by Shuichi Yamamoto; Masaki Nomura; Yuji Sano
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 429 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0009-2509
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β¦ Synopsis
This paper examines how stepwise elution (SE) chromatography can work as a method for the purification and the concentration of proteins at the same time. The concentration factors of proteins by SE with ion exchange chromatography (IEC) or hydrophobic interaction chromatography (HIC) columns were measured as a function of the feed volume and the fed concentration. The experimental results are in good agreement with the calculated ones on the basis of the adsorption isotherm data. The recovery of aamylase from the fermentation broth by SE-HIC was successfully carried out on the basis of the data obtained from the linear gradient elution experiments. The concentration factor obtained was 30-fold while the purification factor w& 23-fold.
π SIMILAR VOLUMES
## Abstract Protein elution curves in ion exchange chromatography (IEC) were simulated with a rate model. Three pure proteins and their mixture were used (Ξ±βlactalbumin, BSA, and conalbumin) under different operational conditions. The anionic matrix QβSepharose FF was used packed in a 1βmL column.
## Abstract Chickens were immunised with peanut protein extracts. Because of the high cross reactivity, the lgY antibodies were purified by means of an affinity column. An ion chromatographically purified peanut protein fraction was therefore coupled to the affinity support material and this column