The effects of nonenzymatic glycation on the binding capacity of beef myofibrillar proteins (MP) to aldehyde flavour compounds were investigated. The binding capacity was significantly increased due to the partial unfolding and flexible secondary structure of the glycated MP. Unfolding played a dominant role in binding due to the prevention of protein aggregation by steric hindrance originating from glycation with glucose (Glu), while glycation with glucosamine (GluA) induced substantial aggregation due to cross-linking. Therefore, the MP glycated with Glu had a higher binding capacity for aldehyde flavour compounds compared to MP glycated with GluA. In a competitive binding system, the MP glycated with Glu had a higher binding capacity for long-chain aldehyde flavour compounds. However, the MP glycated with GluA had a higher binding capacity for short-chain aldehyde flavour compounds, which were more likely to interact with the binding sites shielded in the protein aggregate. Nonenzymatic glycation represents a potential method to enhance the flavour intensity of meat products with high-protein levels.

研究了非酶糖基化对牛肉肌原纤维蛋白（MP）与醛味化合物的结合能力的影响。结合能力由于糖化MP的部分展开和柔性二级结构而显着增加。由于通过阻止由葡萄糖（Glu）糖基化引起的空间位阻而阻止蛋白质聚集，因此展开作用在结合中起主要作用，而由于交联，由葡萄糖胺（GluA）引起的糖基化诱导大量聚集。因此，与用GluA糖化的MP相比，用Glu糖化的MP对醛味化合物具有更高的结合能力。在竞争性结合系统中，用Glu糖基化的MP对长链醛类香精化合物具有更高的结合能力。然而，用GluA糖化的MP对短链醛味化合物的结合能力更高，它们更可能与蛋白质聚集体中被保护的结合位点相互作用。非酶糖基化是增强具有高蛋白水平的肉制品的风味强度的潜在方法。