Lim Woobin, Jeong Yulim, Lee Wonjae, Yoo Byoungseung
Department of Food Science and Biotechnolgy, Dongguk University-Seoul, Goyang, Gyeongggi 10326 South Korea.
Food Sci Biotechnol. 2023 Nov 6;33(6):1407-1412. doi: 10.1007/s10068-023-01447-2. eCollection 2024 May.
High-protein powders (milk protein isolate (MPI) and soybean protein isolate (SPI)) were treated with maltodextrin solution (10% or 20%) or water as a binder and then subjected to fluidized-bed agglomeration. The MPI agglomerates were compared with the SPI agglomerates as a function of maltodextrin (MD) concentration. The particle size, wettability, and porosity values of SPI agglomerates were much higher than those of the raw powder when compared to the MPI agglomerates. The agglomerated protein powders with MD binder showed significantly higher solubility values than the raw powders. These tendencies were discernible in the morphological examination via SEM analysis. The dynamic modulus values of SPI agglomerates decreased with an increase in MD concentration from 10 to 20% whereas those of MPI agglomerates increased. These findings indicate that the physical, structural, and rheological properties of agglomerated high-protein powders are greatly influenced by the type of protein and the addition of MD binder.
将高蛋白粉末（乳清分离蛋白（MPI）和大豆分离蛋白（SPI））用麦芽糊精溶液（10%或20%）或水作为粘合剂进行处理，然后进行流化床团聚。将MPI团聚物与SPI团聚物作为麦芽糊精（MD）浓度的函数进行比较。与MPI团聚物相比，SPI团聚物的粒径、润湿性和孔隙率值远高于原料粉末。用MD粘合剂制成的团聚蛋白粉末的溶解度值明显高于原料粉末。通过扫描电子显微镜（SEM）分析进行的形态学检查中可以看出这些趋势。SPI团聚物的动态模量值随着MD浓度从10%增加到20%而降低，而MPI团聚物的动态模量值则增加。这些发现表明，团聚高蛋白粉末的物理、结构和流变学性质受到蛋白质类型和MD粘合剂添加量的极大影响。
