resumo
Here, circular dichroism (CD) spectroscopy, fluorescence spectroscopy, UV-Vis spectroscopy, SDS-PAGE, substrate SDS-PAGE, and molecular dynamics (MD) simulations techniques have been employed to understand the structural behavioral changes of trypsin (MW: 19.72 kDa, source: digestive system of adult Indian major carp, Catla C. catla) in the presence of various chemical environments. The stability of the trypsin can be increased by stabilizers, including trimethylamine N-oxide (TMAO), proline, and betaine, without affecting its native structure. Trypsin has shown unusual high thermal stability in the presence of betaine. Further, these experimental results were confirmed by means of MD simulations. The present results explicitly elucidated that the behavior of a co-solvent may vary depending upon the type of the protein.
palavras-chave
TRIMETHYLAMINE-N-OXIDE; UREA-INDUCED DENATURATION; ALPHA-CHYMOTRYPSIN; TRYPTOPHAN FLUORESCENCE; GUANIDINE-HYDROCHLORIDE; PROTEIN STABILITY; GLYCINE BETAINE; PREFERENTIAL INTERACTIONS; CIRCULAR-DICHROISM; OSMOLYTES
categoria
Chemistry
autores
Reddy, PM; Taha, M; Sharma, YVRK; Venkatesu, P; Lee, MJ
nossos autores
Mohamed Taha Ahmed Amin
Bolseiro de pós-DoutoramentoGrupos
agradecimentos
We gratefully acknowledge the Council of Scientific Industrial Research (CSIR), New Delhi, Department of Science and Technology (DST), New Delhi, Department of Biotechnology (DBT), New Delhi through the grant no. 01(2713)/13/EMR-II, SB/S1/PC-109/2012, no. BT/PR5287/BRB/10/1068/2012, respectively for financial support.