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Relationship between protein characteristics and film‐forming properties of kidney bean, field pea and amaranth protein isolates

Shevkani, Khetan, Singh, Narpinder
International journal of food science & technology 2015 v.50 no.4 pp. 1033-1043
Fourier transform infrared spectroscopy, albumins, ash content, color, denaturation, dispersions, gel chromatography, globulins, heat treatment, kidney beans, opacity, pH, peas, permeability, protein content, protein isolates, protein solubility, temperature, tensile strength, thermal properties, water vapor, zeta potential
This study was undertaken to evaluate physicochemical (colour, protein content, ash content and zeta potential), structural (size exclusion chromatography and thermal properties) and film‐forming properties of kidney bean, field pea and amaranth protein isolates (KBPI, FPPI and AMPI, respectively). Protein content, ash content, zeta potential and denaturation temperature of the isolates ranged from 83.9 to 91.4%, 2.9 to 4.5%, −37.3 to −44.2 mV and 85.5 to 96.2 °C, respectively. Size exclusion chromatography revealed that globulins were prominent proteins in KBPI and FPPI, while AMPI contained both globulins and albumins as major fractions. FPPI showed the highest L* value (88.1), surface charge (zeta potential = –44.2 mV) and protein solubility (80.0–94.2%). Films were prepared from heated (90 °C for 20 min) and unheated protein dispersions of pH 7.0, 8.0 and 9.0 and evaluated for colour, opacity, tensile strength (TS), water‐solubilised matter (WSM) and water vapour permeability (WVP). FPPI films showed the most desirable properties in terms of the highest L* (87.5–90.5), TS (12.6–37.2 MPa) and the lowest opacity (7.1–8.4 A₆₀₀/mm). FT‐IR spectroscopic analysis of the films revealed that alkaline pH and heat treatment unfolded protein molecules. Alkaline pH reduced opacity, while heat treatment improved TS and water resistance (decreased WSM and WVP) of protein films, which varied with the protein isolates.