Soto, Dayana <br/><br/>
Structure-activity relationships on the study of β-galactosidase folding/unfolding due to interactions with immobilization additives: Triton X-100 and ethanol.  [electronic resource] 

 -  International journal of biological macromolecules  Mar 2017 
 - 87-92 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>1879-0003 
<br/><br/><label>Standard No.: </label>10.1016/j.ijbiomac.2016.12.026  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Bacillus--enzymology<br/>Enzyme Stability--drug effects<br/>Enzymes, Immobilized--chemistry<br/>Ethanol--chemistry<br/>Hydrogen-Ion Concentration<br/>Hydrolysis<br/>Models, Molecular<br/>Octoxynol--chemistry<br/>Protein Conformation, alpha-Helical--drug effects<br/>Protein Conformation, beta-Strand--drug effects<br/>Protein Unfolding--drug effects<br/>Structure-Activity Relationship<br/>Surface-Active Agents--chemistry<br/>Temperature<br/>beta-Galactosidase--chemistry