Synthesis and functionality of proteinacious nutraceuticals from casein whey—A clean and safe route of valorization of dairy waste

Abstract

Due to stricter environmental legislation, coagulation and precipitation technologies have been practiced for whey protein sedimentation from a long prior. Nowadays, in pharmaceutical and dairy industries, individual whey proteins have been isolated by size-exclusion membrane separation technology, ion-exchange membrane chromatography, gel-permeation chromatography, affinity-peptide ligand chromatography and electro-chromatography. Furthermore, whey protein-derived peptides have been synthesized by conventional batch or catalyst-immobilized packed-bed bioreactors or membrane-assigned bioreactor with high throughput and purity, considering raw whey or isolated individual protein as feedstock. Different types of enzymes, such as trypsin, chymotrypsin, alcalase, pepsin and chymosin, have been popularly used for enzymatic hydrolysis of whey proteins. Whey proteins, such as β-lactoglobulin, α-lactalbumin, bovine serum albumin, lactoperoxidase, lactoferrin and immunoglobulins, and enzymatic hydrolysis of whey proteins have their unique physiological, medicinal, functional and nutritional values. It could be expected that without going for mere treatment of whey (coagulation or sedimentation of whole protein), synthesis of proteinacious bioactives (separation of individual whey proteins and synthesis of their derivatives) will lead to zero effluent discharge within a domain of whey upgradation. The present review pretends to highlight the different process-related technological aspects for the synthesis of different proteinacious bioactives from whey, as well as their functionality.