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Title: Diffusion behavior of lysozyme in aqueous ammonium sulfate solutions under varying solution conditions as determined by dynamic light scattering

Technical Report ·
OSTI ID:7092350
; ; ;  [1]
  1. Univ. of California, Berkeley, CA (United States). Dept. of Chemical Engineering Lawrence Berkeley Lab., CA (United States). Chemical Sciences Div.

As proteins gain significance in commercial applications such as pharmaceuticals, detergents, organic waste management and cosmetics, efficient and economical recovery of these valuable biomolecules is of increasing importance. the salting-out process has found widespread application in the area of protein separations. To date, salt-induced precipitation of proteins from complex aqueous solutions remains largely an empirical process; no comprehensive model exists to predict salting-out phase equilibria in protein solutions. Rational predictive models for salt-induced precipitation will therefore be of great value in protein purification, both on the preparative and the analytical scale. Any attempt to model theoretically salt-induced protein precipitation must include the known physics of protein interactions in aqueous solution. With this in mind, it is crucial to acknowledge that protein precipitation is fundamentally an aggregation process. In order to incorporate aggregation effects into ongoing efforts to model salting out of proteins, it is necessary to quantify the degree of aggregation as a function of solution conditions. Therefore, dynamic light scattering measurements were performed with a well-studied protein, hen-egg-white lysozyme, under several solution conditions.

Research Organization:
Lawrence Berkeley Lab., CA (United States)
Sponsoring Organization:
USDOE; National Science Foundation (NSF); USDOE, Washington, DC (United States); National Science Foundation, Washington, DC (United States)
DOE Contract Number:
AC03-76SF00098
OSTI ID:
7092350
Report Number(s):
LBL-36510; ON: DE95004821
Country of Publication:
United States
Language:
English