Correlating Bromelain's activity with its structure and active-site dynamics and the medium's physical properties in a hydrated deep eutectic solvent

Abstract

Deep eutectic solvents (DES) are emerging as the new media of choice for biocatalysts due to its environmentally amiable nature, fine-tunability and potential biocompatibility. This work deciphers the behaviour of...

Macromolecular crowding: how shape and interaction affect the structure, function, conformational dynamics and relative domain movement of a multi-domain protein

“…74 Among various protein dynamics, active site conformational dynamics in the microsecond timescale is believed to be a crucial factor that dictates its function and other properties. 68,[97][98][99][100] In the presence of all the three crowders used in the study, the conformational fluctuation time increases gradually with increasing crowder concentration (see Fig. 5(g)-(i)), suggesting a crowder imposed restriction of the conformational fluctuation of HSA.…”

Current understanding and insights towards protein stabilization and activation in deep eutectic solvents as sustainable solvent media

“…The proteins or enzymes which have been covered here are, collagen, 148–151 keratin, 152–155 subtilisin, 112 chondroitinase ABCI (cABCI), 156 chicken villin headpiece subdomain (HP 36), 157 human interferon-α2 (IFN), 158 β-glucosidase, 159 β-lactamase, 160 transferrin, 161 bovine ribonuclease A (RNase A), 42 β-galactosidase, 162 papain, 163 pepsin, 164 Trp-cage mini protein 165 and bromelain. 30…”

“…Very recently one more aspect of protein dynamics and behaviour in DESs was presented by Das et al 30 The authors employed one of the essential industrial proteolytic enzymes, bromelain, to study its behaviour in a ternary DES composed of acetamide–urea–sorbitol with mole fractions of 0.5, 0.3 and 0.2 respectively, at various hydration levels. The research work highlighted that, at lower concentrations of DES, the enzyme was slightly in a more compact state, whereas at higher concentrations the structure gets elongated.…”

“…There are only a handful of reports available related to protein stability and refolding ability in DESs. 2,12,16,30,39–42 The recent studies published by our group reveal that DESs exhibit outstanding properties such as solubility, stability of proteins and enzyme activation in these solvents. The investigation validates DESs as biocompatible media by imparting stabilization, activity enhancement and thermal preservation to proteins.…”

“…2,8,23–26 These green solvents have prompted exclusive opportunities in studies dealing with protein-refolding, increasing the shelf life, improving the enzymatic activity, enhancing the thermal stability and sustainable biomolecular extraction processes, and many more. 8,27–31…”