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A Dynamic Light Scattering Study of β‐Galactosidase: Environmental Effects on Protein Conformation and Enzyme Activity
Author(s) -
Yang ShangTian,
Marchio Jack L.,
Yen JyhWen
Publication year - 1994
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00029a011
Subject(s) - dynamic light scattering , chemistry , enzyme , protein aggregation , particle size , substrate (aquarium) , biophysics , light scattering , enzyme assay , lactose , biochemistry , scattering , materials science , biology , nanotechnology , optics , physics , nanoparticle , ecology
Dynamic light scattering (DLS) is a useful technique for analyzing the size, shape, and other structural characteristics of protein molecules in solution. The effects of various environmental conditions on the structure and activity of Aspergillus oryza e β‐galactosidase were studied. DLS was used to determine protein particle size under various salt, pH, and temperature conditions. Changes in the activity and stability of this enzyme caused by different environmental conditions were found to correlate well with the size changes of the protein particles. This change in protein size can be attributed to protein unfolding and aggregation under extreme conditions. The presence of the enzyme substrate, lactose, in the protein solution greatly enhanced enzyme stability by inhibiting aggregation.