Luo Jie, Wang Yuhan, Guo Huiyuan, Ren Fazheng
Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural Univ., China.
Key Laboratory of Functional Dairy, Co-constructed by Ministry of Education and Beijing Government, College of Food Science and Nutritional Engineering, China Agricultural Univ., China.
J Food Sci. 2017 Mar;82(3):670-678. doi: 10.1111/1750-3841.13649.
Rennet-induced gelation crucially impacts cheese structure. In this study, effects of the size and stability of native fat globules on the kinetics of rennet-induced coagulation were revealed by determining the caseinomacropeptide release rate and rheological properties of milk. Moreover, the mobility and stability of fat globules during renneting was revealed using diffusing wave spectroscopy and confocal laser scanning microscopy. By use of a 2-stage gravity separation combined centrifugation scheme, native fat globules were selectively separated into small (SFG, D = 1.87 ± 0.02 μm) and large fat globules (LFG, D = 5.65 ± 0.03 μm). The protein and fat content of SFG and LFG milk were then standardized to 3.2 g/100 mL and 1.2 g/100 mL, respectively. The milk containing different sized globules were then subjected to renneting experiments in the laboratory. Reduction of globule size accelerated the aggregation of casein micelles during renneting, giving a shorter gelation time and earlier 1/l change. The gel produced from LFG milk was broken due to coalescent fat globules and generated coarser gel strands compared to the finer strands formed with SFG milk. Structural differences were also confirmed with a higher final storage modulus of the curd made from SFG milk than that from the LFG. In conclusion, the size of fat globules affects the aggregation of casein micelles. Moreover, fat globule coalescence and creaming during renneting, also affects the structure of the rennet gel. A better understanding of the size of globules effect on milk gelation could lead to the development of cheese with specific properties.
凝乳酶诱导的凝胶化对奶酪结构至关重要。在本研究中,通过测定酪蛋白巨肽释放速率和牛奶的流变学特性,揭示了天然脂肪球的大小和稳定性对凝乳酶诱导的凝固动力学的影响。此外,使用扩散波谱和共聚焦激光扫描显微镜揭示了凝乳过程中脂肪球的流动性和稳定性。通过采用两阶段重力分离结合离心方案,将天然脂肪球选择性地分离为小脂肪球(SFG,直径D = 1.87 ± 0.02μm)和大脂肪球(LFG,直径D = 5.65 ± 0.03μm)。然后将SFG和LFG牛奶的蛋白质和脂肪含量分别标准化为3.2 g/100 mL和1.2 g/100 mL。然后将含有不同大小脂肪球的牛奶在实验室中进行凝乳酶处理实验。脂肪球尺寸的减小加速了凝乳过程中酪蛋白胶束的聚集,从而缩短了凝胶化时间并提前出现1/l变化。与SFG牛奶形成的较细凝胶链相比,LFG牛奶产生的凝胶因脂肪球聚结而破裂,并产生更粗的凝胶链。用SFG牛奶制成的凝乳的最终储能模量高于LFG制成的凝乳,这也证实了结构上的差异。总之,脂肪球的大小会影响酪蛋白胶束的聚集。此外,凝乳过程中脂肪球的聚结和上浮也会影响凝乳酶凝胶的结构。更好地理解脂肪球大小对牛奶凝胶化的影响可能会导致开发出具有特定特性的奶酪。