Structure-activity relationships on the study of β-galactosidase folding/unfolding due to interactions with immobilization additives: Triton X-100 and ethanol

详细信息    查看全文

• 作者：Dayana Soto^a ; Sindy Escobar^a ; Fanny Guzmá ; n^b ; Constanza Cá ; rdenas^b ; Claudia Bernal^c ; Monica Mesa^a ; ^{monica.mesa@udea.edu.com} ; ^{mesacad@gmail.com}
• 关键词：BgaC ; β&ndash ; galactosidase from Bacillus circulans ; CD ; Circular Dichroism ; DSC ; Differential Scanning Calorimetry ; FTIR ; Infrared spectroscopy
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：96
• 期：Complete
• 页码：87-92
• 全文大小：1939 K
• 卷排序：96

文摘

Structure-activity relationship (SAR) from Circular Dichroism and β-gal activity. Role of Triton X-100 as stabilizer and ethanol as co-solvent from SAR. SAR result from Short and large range structural changes respecting to active site. Triton X-100 has local and multipoint interactions due to its free and micellar forms. Rationalizing Surfactant-enzyme interactions is the base for stabilizing strategies.