Antimicrobial and antioxidant properties of -conglycinin and glycinin from soy protein isolate
نویسندگان
چکیده
Soybeans (Glycine max) are an abundant source of proteins that have been recognized for their high nutritional value and bioactive properties. Soybeans are legumes, and possess high protein content (approximately 40%) as compared to most other legumes (Aguirre et al., 2008; Yimit et al., 2012). The health benefits of soybeans are attributed to the presence of bioactive compounds, and in particular proteins. Glycinin and -conglycinin are globulins that are the major components of soy protein isolates (SPIs), accounting for approximately 85% of soybean protein content (Scilingo and Añon, 2004; Vernaza et al., 2012). Glycinin is a polypeptide that is composed of 2 acidic and basic subunits that are connected with disulfide bonds. ISSN: 2319-7706 Volume 3 Number 8 (2014) pp. 144-157 http://www.ijcmas.com
منابع مشابه
Bioactive proteins against pathogenic and spoilage bacteria
Glycinin, basic subunit and β-conglycinin were isolated from soybean protein isolate and tested for their antimicrobial action against pathogenic and spoilage bacteria as compared to penicillin. The three fractions exhibited antibacterial activities equivalent to or higher than penicillin in the next order; basic subunit>glycinin> β-conglycinin with MIC of 50, 100 and 1000 μg/mL, respectively. ...
متن کاملImproved fractionation of glycinin and beta-conglycinin and partitioning of phytochemicals.
Glycinin-rich and beta-conglycinin-rich products are prepared by soy protein fractionation. Physicochemical characteristics of these proteins affect their unique, important functionality in food systems and industrial applications. Soybean isoflavones and saponins are phytochemicals with potential health benefits. Objectives of this protein fractionation research were to (1) improve protein and...
متن کاملEffect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate
Changes of structure and thermal stability of soy protein isolate after pulsed electric field treatment were analyzed by Fourier transform infrared spectroscopy and differential scanning calorimetry (DSC). When the applied pulsed electric field (PEF) treatment intensity was over 35 kV/cm, the amino acid side chain, anti-parallel b-sheets, b-turn as well as b-sheets in soy protein isolate (SPI) ...
متن کاملAdsorption of glycinin and β-conglycinin on silica and cellulose: surface interactions as a function of denaturation, pH, and electrolytes.
Soybean proteins have found uses in different nonfood applications due to their interesting properties. We report on the kinetics and extent of adsorption on silica and cellulose surfaces of glycinin and β-conglycinin, the main proteins present in soy. Quartz crystal microgravimetry (QCM) experiments indicate that soy protein adsorption is strongly affected by changes in the physicochemical env...
متن کاملHeat-induced aggregation and sulphydryl/disulphide reaction products of soy protein with different sulphydryl contents.
In this study, soy proteins were reduced with 0.1-10mM dithiothreitol (DTT) to obtain an increasing number of sulphydryl groups (SH) with a similar particle size. Aggregation was promoted by increasing the degree of reduction when heated (100°C, 30min), resulting in larger sized aggregates (from 40 to 70nm) and a higher viscosity of the aggregate dispersion. The disulphide bond (SS) content dec...
متن کامل