Ying Qiao , Junli Miao , Yifan Hua , Wei Li , Xuehong Zhang , Zhenmin Liu
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引用次数: 0
Abstract
Residual α-amylase activity in stored pasteurized yogurt hydrolyses hydroxypropyl distarch phosphate (HPDSP), threatening product quality and motivating this study to establish safe enzymatic thresholds for texture stability. Bacillus licheniformis α-amylase (HEa) demonstrated superior thermal stability with a static half-life 5–10 times longer than that of Aspergillus oryzae (ASa) at 85–100 °C. HEa effectively hydrolysed HPDSP, reducing starch residue to 77 % at ultra-trace concentrations of 1.0 × 10−4 U/L, respectively. Conversely, ASa exhibited negligible hydrolysis even at a concentration of 1 U/L. Rheological analysis revealed that elevated α-amylase concentrations significantly decreased yogurt viscosity and yield stress. However, controlled enzyme levels (ASa ≤ 1.0 × 10−1 U/L or HEa ≤ 1.0 × 10−3 U/L) maintained optimal viscosity and shear-thinning behaviour throughout storage. These findings highlight the importance of stringent α-amylase level control to maintain consistent texture and quality in pasteurized yogurt products during storage.
期刊介绍:
Food Chemistry: X, one of three Open Access companion journals to Food Chemistry, follows the same aims, scope, and peer-review process. It focuses on papers advancing food and biochemistry or analytical methods, prioritizing research novelty. Manuscript evaluation considers novelty, scientific rigor, field advancement, and reader interest. Excluded are studies on food molecular sciences or disease cure/prevention. Topics include food component chemistry, bioactives, processing effects, additives, contaminants, and analytical methods. The journal welcome Analytical Papers addressing food microbiology, sensory aspects, and more, emphasizing new methods with robust validation and applicability to diverse foods or regions.