Bio-Molecular Interaction Studies in the System of Pectin + α-amylase at 298.15 K

Abstract

kT Temperature Dependent Constant k Temperature Independent Constant Meff, M Effective Molecular Weight, x Mole Fraction i Component % Percentage m Molecular Weight β Adiabatic Compressibility Lf Free Length Vf Free Volume πi Internal Pressure T Temperature R Universal Gas Constant b Atomic Scaling Factor α Molecular Interaction Parameter ∑ Summation e Percentage Deviation of free length theory [9], Danusso model [10], Junjie’s method [11], and Rao formalism [12] interpreted in the results in terms ofmolecular interactions. There has been increasing interest in the study of intermolecular interactions in several years and numbers of experimental techniques have been used to investigate the interactions between the binary and ternary mixtures components. Ultrasonic studies of liquid mixtures, due to the nondestructive nature, have been extensively carried out in different branches of science (physical, chemical, biological) to measure the thermodynamic properties to predict the nature of molecular interactions between the molecules in a medium. The ultrasonic sound velocity, and the thermodynamic parameters derived from it have been widely used to interpret the interactions between unlike molecules in the binary and ternary mixtures. In the present study, an attempt has been made to study the intermolecular interaction in the binary mixture of pectin with α-amylase solution by measuring the ultrasonic velocity, density, and viscosity of the mixtures at 298.15 K [13]. Various theories and relations suggested by Danusso (1951), Jacobson (1952), Junjie (1984), and Gokalae (1989) are used to calculate the ultrasonic velocity [9–12].