Abstract
The Ceylon Journal of Science is published by the University of Peradeniya, Sri Lanka. Full text available. The journal also has its own website. The Ceylon Journal of Science is a continuation of the Ceylon Journal of Science (Biological Sciences) which is no longer being published as a separate journal. The history of the journal can be found here.From May 2020, Ceylon Journal of Science is indexed in DOAJ.
Highlights
IntroductionLayered Double Hydroxides (LDHs) are well known in immobilizing biologically active materials such as porphyrins (Park et al, 1989; Bonnet et al, 1996; Robbins and Dutta, 1996), nucleoside phosphates (Choy et al, 2000; Choy et al, 2001; Minagawa et al, 2019), drugs (Fardella et al, 1997a; Fardella et al, 1997b; Fardella et al, 1998; Fogg et al, 1998; Khan et al, 2001; Choi et al, 2018), vitamins (Hwang et al, 2001), amino acids (Whilton et al, 1997; Aisawa et al, 2000; Aisawa et al, 2001) and fatty acids (Meyn et al, 1990; Borja and Dutta, 1992)
Three major diffraction peaks were clearly visible in the PXRD patterns obtained for the solid materials and they were characteristic to the basic structure of Layered Double Hydroxides (LDHs)
Sodium Dodecyl Sulphate (SDS) entrapped trypsin gave the highest retention of activity (84.66%) while covalent crosslinking can further be improved
Summary
Layered Double Hydroxides (LDHs) are well known in immobilizing biologically active materials such as porphyrins (Park et al, 1989; Bonnet et al, 1996; Robbins and Dutta, 1996), nucleoside phosphates (Choy et al, 2000; Choy et al, 2001; Minagawa et al, 2019), drugs (Fardella et al, 1997a; Fardella et al, 1997b; Fardella et al, 1998; Fogg et al, 1998; Khan et al, 2001; Choi et al, 2018), vitamins (Hwang et al, 2001), amino acids (Whilton et al, 1997; Aisawa et al, 2000; Aisawa et al, 2001) and fatty acids (Meyn et al, 1990; Borja and Dutta, 1992). Once an enzyme is purified outside its native biological environment, it is liable to denature due to deviations of temperature, pH value, radiation and various other factors. Proteases possess an added affinity to lose its maximum catalytic capacity via destruction of its native protein structure by their own action of proteolysis called autolysis (Koutsopoulos et al, 2007). Autolysis refers to the destruction of a cell through the action of its own enzymes. Trypsin being a protease should be stored at low temperatures (between −20 °C and −80 °C) to prevent autolysis. Autolysis may be prevented by storage of trypsin at pH=3 or by modifing trypsin via reductive methylation. When the pH is adjusted back to pH=8, the activity returns back to normal (Koutsopoulos et al, 2007)
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