Purification of neutral protease by dye affinity chromatography View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-03

AUTHORS

Nancy B. Iannucci, Agustín A. Navarro del Cañizo, Osvaldo Cascone

ABSTRACT

Twenty triazinic dyes were assayed as ligands for the chromatographic affinity purification of a neutral protease from Flavourzyme, a commercial preparation. Screening at pH 4.0 allowed the selection of eight dyes on the basis of their high protease adsorption. When the pH was set to 5.0 in order to increase selectivity, only Yellow HE-4R, Red HE-3B, and Cibacron Blue F3G-A maintained protease adsorption at high values. Neither maximum capacities nor dissociation constants calculated from isotherms measured at 8 and 25 degrees C showed great differences. By contrast, a strong temperature effect was evidenced in the elution step: elution at 8 degrees C allowed 70, 81, and 98% recovery of adsorbed protease with Yellow HE-4R, Red HE-3B, and Cibacron Blue F3G-A, respectively, whereas only 20% recovery was attained at 25 degrees C. Based on the results obtained, a purification process for the neutral protease contained in Flavourzyme with Cibacron Blue F3G-A as the affinity ligand was developed, yielding 96% of electrophoretically pure enzyme in a single step, the specific activity rising from 850 to 3650 U/mg. More... »

PAGES

173-183

Identifiers

URI

http://scigraph.springernature.com/pub.10.1385/abab:104:3:173

DOI

http://dx.doi.org/10.1385/abab:104:3:173

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034425810

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12665669


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