Marino Rosaria, Della Malva Antonella, Caroprese Mariangela, De Pilli Teresa, Alessandrino Ofelia, Picariello Gianluca, Sevi Agostino, Albenzio Marzia
Department of Agriculture, Food, Natural Resources and Engineering (DAFNE), University of Foggia, Via Napoli, 25-71121 Foggia, Italy.
Department of Agriculture, Food, Natural Resources and Engineering (DAFNE), University of Foggia, Via Napoli, 25-71121 Foggia, Italy.
Meat Sci. 2023 Jun;200:109147. doi: 10.1016/j.meatsci.2023.109147. Epub 2023 Feb 22.
The impact of papain and/or ultrasound treatments on tenderization of semitendinosus muscle through a proteomic approach was studied. Sixteen bovine muscles were submitted to the following treatments: aging at 3 °C (Control), papain injection (PI), ultrasound (US), PI followed by US (PIUS) and US followed by PI (USPI). pH, myofibrillar fragmentation indices (MFI), soluble collagen, texture profile and changes of myofibrillar proteins were investigated after 2, 24, 48 and 96 h of storage. The highest MFI and soluble collagen content were found in PI, PIUS and USPI samples while control samples showed the lowest values. PI samples showed the lowest WBSF and hardness values until 48 h of storage while at 96 h meat from USPI treatment showed WBSF value comparable to PI treatment. The lowest values of cohesiveness, gumminess and chewiness were found in PI samples during all storage times. Proteomic analysis revealed a different quantity and expression of proteins among tenderization treatments. US treatment did not exhibit a significant ability to degrade muscle proteins, while, all treatments containing papain, showed a greater ability to hydrolyse and degrade myofibrillar proteins. PI promoted intense proteolysis leading to an early tenderization process; on the contrary, in PIUS and USPI treatments the sequence of treatments was relevant on meat tenderization. Particularly, USPI treatment, after 96 h, reached the same improvement in tenderness of enzymatic treatment but with slower hydrolysing rate; this could be determinant to preserve textural structure.
通过蛋白质组学方法研究了木瓜蛋白酶和/或超声处理对半腱肌嫩化的影响。将16块牛肌肉进行以下处理：在3°C下成熟（对照）、注射木瓜蛋白酶（PI）、超声处理（US）、先注射木瓜蛋白酶后进行超声处理（PIUS）以及先进行超声处理后注射木瓜蛋白酶（USPI）。在储存2、24、48和96小时后，研究了pH值、肌原纤维破碎指数（MFI）、可溶性胶原蛋白、质地剖面和肌原纤维蛋白的变化。在PI、PIUS和USPI样品中发现了最高的MFI和可溶性胶原蛋白含量，而对照样品的值最低。直到储存48小时，PI样品的Warner-Bratzler剪切力值（WBSF）和硬度值最低，而在96小时时，USPI处理的肉的WBSF值与PI处理相当。在所有储存时间内，PI样品的内聚性、胶黏性和咀嚼性值最低。蛋白质组学分析揭示了嫩化处理之间蛋白质的数量和表达存在差异。超声处理没有表现出显著降解肌肉蛋白质的能力，而所有含木瓜蛋白酶的处理都表现出更强的水解和降解肌原纤维蛋白的能力。PI促进了强烈的蛋白水解，导致早期嫩化过程；相反，在PIUS和USPI处理中，处理顺序对肉的嫩化有影响。特别是，USPI处理在96小时后达到了与酶处理相同的嫩度改善，但水解速率较慢；这可能是保持质地结构的决定性因素。
