Alpizar-Reyes E, Castaño J, Carrillo-Navas H, Alvarez-Ramírez J, Gallardo-Rivera R, Pérez-Alonso C, Guadarrama-Lezama A Y
1Facultad de Química, Universidad Autónoma del Estado de México, Paseo Colón esq. Paseo Tollocan s/n, Col. Residencial Colón, C.P. 50120 Toluca, Estado de México Mexico.
2Unidad de Desarrollo Tecnológico, Universidad de Concepción, Avenida. Cordillera, C.P 2634 Coronel, Republic of Chile.
J Food Sci Technol. 2018 Mar;55(3):935-943. doi: 10.1007/s13197-017-3001-1. Epub 2018 Jan 27.
Freeze-dried faba bean ( L.) protein adsorption isotherms were determined at 25, 35 and 40 °C and fitted with the Guggenheim-Anderson-de Boer model. The pore radius of protein was in the range of 0.87-6.44 nm, so that they were considered as micropores and mesopores. The minimum integral entropy ranged between 4.33 and 4.44 kg HO/100 kg d.s., was regarded as the point of maximum of stability. The glass transition temperature of the protein equilibrated at the different conditions of storage was determined, showing that the protein remained in glassy state for all cases. The protein showed compact and rigid structures, evidenced by microscopy analysis.
测定了冻干蚕豆（L.）蛋白在25、35和40°C下的吸附等温线，并采用古根海姆-安德森-德布尔模型进行拟合。蛋白质的孔径在0.87 - 6.44纳米范围内，因此被视为微孔和中孔。最小积分熵在4.33至4.44千克水/100千克干物质之间，被视为最大稳定性点。测定了在不同储存条件下平衡的蛋白质的玻璃化转变温度，结果表明在所有情况下蛋白质都保持玻璃态。显微镜分析表明，该蛋白质呈现紧密而刚性的结构。
