Soy proteins and their modifications in different food formulations

Dr.A.P.Gandhi B.Sc(Ag),M.Sc,Ph.D,Post Doctorate(Denmark & USA) Principal Scientist (Biochemistry) Central Institute of Agricultural Engineering Bhopal-462038(MP)

Soybean proteins are being popularized and getting the utmost importance due to many fold qualities like good functional properties, varied food applications, high nutritional significance, readily available and in expensive. The major storage proteins in soybean are globulins. These are four protein fractions namely 2S, 5S, 7S and 11S comprising approximately 8%, 35%, 52% and 5% of the total proteins respectively. Among them 7S and 11S are the principal storage proteins. The 11S proteins are glycin. It is a protein with a compact quaternary structure stabilized by disulfide, electrostatic and hydrophobic interactions. Its molecular weight is 360 kDa. It is made of six A-SS-B sub units. Each unit is composed of an acid (m.w about 38 kDa) and basic poly peptide (m.w. about 20kDa). They are linked by single disulfide bond except for the acid poly peptide. All the sub units are packed into hexagons placed one over the other to form a hollow structure. Beta conglycinin is the major protein of 7S fraction. With a molecular weight of 150-180 kDa. It is composed of three sub units alpha-1, alpha-2 and beta which in turn produce seven isomers (B0-B6). The molecular weight of these sub units is 72kDa, 68kDa and 52kDa respectively. It is a glycoprotein and contains carbohydrates as one unit attached to aspartic acid at the N terminal end of the molecule. The carbohydrate contains about 38 mannose and 12 glucosamine residues per molecule of protein. 11S protein is insoluble at pH 6.4 where as beta conglycinin is insoluble at pH 4.8 and 2-5oC. The nutritional, physico chemical and functional properties of soy and soy based protein products may be changed by various physical, chemical and enzymatic treatments as designed in the process. These treatments include heating, pH shocks, hydrolysis and covalent attachment. Heat treatments: Soybeans contain unusually large number of biologically active components like proteolytic inhibitors, certain enzymes and off flavor causing organic molecules. Thermal treatments reduce them and improve specific functional properties bedsides improving the digestibility of proteins. Heating above 70oC causes disassociation of their quaternary structures, denatures their sub units and promotes the formation of protein aggregates via electro static, hydrophilic and disulfide inters change mechanism. Glycin has a higher thermal transition point ( 92oC) than beta conglycin ( 72oC).The proteolytic inhibitor activity in soybean is mainly due to Kunitz Inhibitor (KI) and Bowman Birk Inhibitor (BBI). They cause pancreatic hypertrophy and hyperplasia. Depending up on the genomes, soybeans have not more than three isomers of KI and 5-12 isomers of BBI. KI consists of 181 amino acid residues with two disulfide bridges. BBI is a low molecular weight protein (7-8 kDa) consisting of 70-80 amino acid residues with seven disulfide bridges. It is rich source of sulfur. They represent 8-10% of the total proteins in soybean but cause about 40% of adverse effect raw soybean consumption. Different modes of heat treatments like live steam treatment (toasting/heating at different steam pressures), cooking, roasting, dielectric and microwave heating are in vogue to reduce the impact of these inhibitors. It is well established that dry heat has no significant reducing effect on these inhibitors even at

121oC. On the other hand treatments with steam over a range of 0.5-2.0 bars, steam jet cooking and autoclaving are more effective. In the modern are the microwave heating at 620W-240MHz for only two minutes reduced the inhibitor activity to 13.33%. High Pressure treatments: Soy proteins are very sensitive to the static high pressure. Intra molecular hydrophobic and electrostatic interactions are disrupted by the application of high pressure with important consequences for the tertiary and quaternary structures of protein. The static high pressure (200-600 MPa) alters the quaternary structure of the 11S increasing the protein-protein interactions and the interactions between the globulins and poly saccharides present. It disassociates the 7S. Chemical treatments: Chemical modifications reduce the inhibitor activity, reduction in phytic acid, increase or decrease of protein solubility to get better, functional properties, to increase nutritive value by covalent binding of amino acids with sulfur and eliminate the undesirable color and flavor. The globular proteins have minimum solubility at pH 4.0-5.0. Acidification to pH 4.0-4.2 insolubilizes about 90% proteins. Solubility increases at pH 11-12. However toxic products like lysinoalanine could be produced at these pH values. Hence mild alkaline modifications (pH 8.0) at slightly increased temperature (50-60oC) may be adopted to produce better solubility in product formulations. The inhibitors may be inactivated by cleavage of two disulfide bridges in KI and four of BBI. Sulfiting agents like sodium meta bisulfite (0.05M-1M) at increased temperature ( 75oC) reduced the activities to 75-94% and with combination of glutaraldehyde up to 99% in one hour. The former cleaves the disulfide bonds and the later interacts with the reactive groups of active sites of the inhibitors. Enzyme modification is also being carried out. Enzymes like proteases break the bonds between protein and volatile compounds. Some oxidizes oxidize aldehydes irreversibly and the end products could be easily removed. This improves the off flavors associated with the soy based foods. The peptides produced by the partial hydrolysis contribute to increased functional properties such as solubility, foaming, gelling and emulsifying.