Brishti Fatema Hossain, Chay Shyan Yea, Muhammad Kharidah, Ismail-Fitry Mohammad Rashedi, Zarei Mohammad, Karthikeyan Sivakumaran, Saari Nazamid
Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
Department of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
Food Res Int. 2020 Dec;138(Pt B):109783. doi: 10.1016/j.foodres.2020.109783. Epub 2020 Oct 15.
Mung bean is an inexpensive yet sustainable protein source. Current work compared the effects of freeze (FD), spray (SD) and oven drying (OD), on mung bean protein isolate (MBPI) produced on pilot scale. All samples showed no dissociation of protein subunits and were thermally stable (T = 157.90-158.07 °C). According to morphological studies, FD formed a porous protein while SD and OD formed wrinkled and compact crystals, respectively. FD and SD formed elastic gels with better gelling capacity than OD (aggregated gel). FD showed exceptional protein solubility, water and oil absorption capacity (4.23 g/g and 8.38 g/g, respectively). SD demonstrated the smallest particle size, excellent emulsion activity index (29.21 m/g) and stability (351.90 min) and the highest β-sheet amount (37.61%). FTIR spectra for all samples showed characteristic peaks which corresponded well to the secondary structure of legume proteins. Rheological analysis revealed that gelation temperature for all MBPI lied around 90 °C. Current work described the different final properties achieved for MBPI produced under different drying techniques that allowed tailoring for different food systems, whereby FD is ideal for meat extender, SD is suitable for meat emulsion while OD is suitable in general protein-based application.
绿豆是一种价格低廉但可持续的蛋白质来源。目前的研究比较了冷冻干燥(FD)、喷雾干燥(SD)和热风干燥(OD)对中试规模生产的绿豆分离蛋白(MBPI)的影响。所有样品的蛋白质亚基均未解离,且具有热稳定性(T = 157.90 - 158.07℃)。形态学研究表明,冷冻干燥形成了多孔蛋白,而喷雾干燥和热风干燥分别形成了有褶皱的紧密晶体。冷冻干燥和喷雾干燥形成了弹性凝胶,其凝胶能力优于热风干燥形成的凝胶(聚集凝胶)。冷冻干燥表现出优异的蛋白质溶解性、水和油吸收能力(分别为4.23 g/g和8.38 g/g)。喷雾干燥的颗粒尺寸最小,具有优异的乳化活性指数(29.21 m/g)和稳定性(351.90分钟),且β-折叠含量最高(37.61%)。所有样品的傅里叶变换红外光谱显示出与豆类蛋白质二级结构良好对应的特征峰。流变学分析表明,所有绿豆分离蛋白的凝胶化温度约为90℃。目前的研究描述了在不同干燥技术下生产的绿豆分离蛋白所具有的不同最终特性,这些特性可针对不同的食品体系进行调整,其中冷冻干燥适用于肉类增量剂,喷雾干燥适用于肉糜,而热风干燥一般适用于基于蛋白质的应用。