Self‐polymerization of optimized amount of 2‐hydroxyethylmethacrylate (HEMA) in a natural deep eutectic solvent (NADES) is obtained by the complexation between choline chloride and fructose (ChCl:Fruc. 2:1) in the presence of indomethacin, an anti‐inflammatory drug resulted formation of a drug‐immobilized ion gel. The ion gel thus obtained is found to be stable in gastrointestinal fluid pH (GIF) and sustained release in simulated lower intestinal fluid for 20 h (88% release) at pH 6.8 and 96% release at pH 7.4 for 15 h (colon & blood pH) at physiological human body temperature (37 °C) of the drug is recorded. The drug can be stored in the gel matrices at room temperature for long durations such as 6 months without any degradation. The ion gel of poly‐HEMA obtained in the NADES does not appear to inhibit the growth of mammalian cells in vitro and is found to be compatible to human blood thus implying toward their potential for therapeutic applications as pH‐sensitive hydrophobic drug carrier for oral application as well as in tissue engineering.

β-Galactosidase from halotolerant Aspergillus tubingensis GR1 was purified by two-step purification process comprising ammonium sulfate precipitation followed by size exclusion chromatography (SEC). The recovery of β-galactosidase after SEC was found to be 1.40% with 58.55-fold increase in specific activity. The molecular weight of β-galactosidase protein was found to be 93 kDa by SDS-PAGE. Activation energy for O-nitrophenol β-D-galactopyranoside (ONPG) hydrolysis was 32.88 kJ mol(-1), while temperature quotient (Q(10)) was found to be 1.375. The enzyme was found to be stable over wide pH range and thermally stable at 60-65°C up to 60 min of incubation while exhibited maximum activity at 65°C with pH 3.0. V(max), K(m), and K(cat) for ONPG were found to be 2000 U ml(-1), 8.33 mM (ONPG), and 101454 s(-1), respectively. Activation energy for irreversible inactivation Ea(d) of β-galactosidase was 100.017 kJ mol(-1). Thermodynamic parameters of irreversible inactivation of β-galactosidase and ONPG hydrolysis were also determined. However, β-galactosidase enzyme activity was activated significantly in the presence of 15% NaCl and hence shows activity up to 30% NaCl concentration.

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