Non-equilibrium Binding Energy Determined Using Alpha-amylase Catalysed Amylolysis of Gelatinised Starch as a Probable Generalisable Model and Importance

Non-equilibrium Binding Energy Determined Using Alpha-amylase Catalysed Amylolysis of Gelatinised Starch as a Probable Generalisable Model and Importance Ikechukwu I. Udema

Objectives: This research was undertaken to determine the non–equilibrium binding energy by calculation after substituting experimental data into derived equations, present its role distinct from energy associated with activated enzyme–substrate (ES) complex and ultimately elucidate the importance of binding energies. Background: There are overwhelming pieces of evidence in the literature that binding interaction is essential for the ultimate transformation of a substrate, inhibition of vital enzymes of pathogens, covid-19 in particular. Intrinsic binding energy herein referred to as non–equilibrium binding energy and energy associated with activated ES are seen to be chemical in origin. Much attention seemed not to be given to theoretical approach to the determination of non–equilibrium binding energy. Methods: Experimental approach (Bernfeld method of enzyme assay) and calculational. Results and Discussion: The non–equilibrium translational (2.691–2.726 kJ/mol) and total electrostatic energies (2.755-3.154 kJ/mol) were > than the thermal energy at 310.15 k. The interfacial distance between the bullet and target molecule was expectedly very short; the range was between 6.672 and 7.570 exp (- 12) m. This was attributed to the interaction between charged enzyme and weakly polar substrate. Conclusion: The equations of non–equilibrium and translational energies were derivable. The binding interaction serves to fix the bullet molecule on or into the target (supra) molecule before the commencement of transition state formation. The non–equilibrium binding interactions of the bullet (drugs, substrate, etc) and target (receptors e.g. enzymes, pathogens such as Covid–19, Plasmodium etc) and the ultimate complex are likely to be stabilised against the thermal energy in furtherance of enzymatic and drug action since the electrostatic interaction energy is higher than thermal energy.
09 19 2020 9 23 10.9734/ajocs/2020/v8i319044 https://journalajocs.com/index.php/AJOCS/article/view/118 https://www.journalajocs.com/index.php/AJOCS/article/download/19044/35118 https://www.journalajocs.com/index.php/AJOCS/article/download/19044/35118 https://www.journalajocs.com/index.php/AJOCS/article/download/19044/35119