Kowalik Jarosław, Tarapata Justyna, Lobacz Adriana, Zulewska Justyna
Department of Dairy Science and Quality Management, Faculty of Food Science, University of Warmia and Mazury in Olsztyn, Oczapowskiego 7, 10-719 Olsztyn, Poland.
Foods. 2024 Oct 17;13(20):3296. doi: 10.3390/foods13203296.
This study investigated the production of rennet gels from β-casein-depleted retentates obtained through cold microfiltration (MF) of skim milk (SM) that was treated beforehand to ensure microbial safety. The treatments included thermization (65 °C, 20 s), pasteurization (72 °C, 15 s), and microfiltration (50 °C; 1.4 μm pore size). The reduction in β-casein content was 0.98, 0.51 and 0.90%, respectively. All treatments resulted in the partial aggregation of serum proteins, which were slightly concentrated in the retentates obtained post cold MF process. This aggregation, along with concentration effect, likely inhibited β-casein dissociation from casein micelles and permeation, particularly in pasteurized milk. Renneting and coagulation properties of the retentates were comparable to those of the respective SM samples, with no significant differences in syneresis, water-holding capacity, or protein hydration. Notably, the retentate from thermized SM, which showed the best performance with the highest β-casein reduction (0.98%), demonstrated shorter coagulation time compared to retentate from pasteurized milk or the corresponding unfiltered SM. Textural analysis revealed greater firmness, cohesiveness, and viscosity of retentate-based rennet gels compared to gels made from unfiltered SM, attributed to protein concentration during cold MF. Overall, this study successfully produced rennet gels from cold MF retentates without compromising their physicochemical properties.
本研究调查了通过对预先处理以确保微生物安全的脱脂乳(SM)进行冷微滤(MF)获得的β-酪蛋白耗尽截留物制备凝乳酶凝胶的情况。处理包括预热(65℃,20秒)、巴氏杀菌(72℃,15秒)和微滤(50℃;孔径1.4μm)。β-酪蛋白含量的降低分别为0.98%、0.51%和0.90%。所有处理均导致血清蛋白部分聚集,这些蛋白在冷微滤过程后获得的截留物中略有浓缩。这种聚集以及浓缩效应可能抑制了β-酪蛋白从酪蛋白胶粒的解离和渗透,尤其是在巴氏杀菌乳中。截留物的凝乳酶作用和凝固特性与相应的脱脂乳样品相当,在脱水收缩、持水能力或蛋白质水合方面无显著差异。值得注意的是,预热脱脂乳的截留物表现出最佳性能,β-酪蛋白降低率最高(0.98%),与巴氏杀菌乳的截留物或相应的未过滤脱脂乳相比,其凝固时间更短。质地分析表明,与由未过滤脱脂乳制成的凝胶相比,基于截留物的凝乳酶凝胶具有更高的硬度、内聚性和粘度,这归因于冷微滤过程中的蛋白质浓缩。总体而言,本研究成功地从冷微滤截留物中制备了凝乳酶凝胶,且不影响其理化性质。