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牛肉里脊(腰大肌)和牛里脊(腰最长肌)中源自蛋白质的肽在冷藏过程中的定量变化。

Quantitative changes in peptides derived from proteins in beef tenderloin (psoas major muscle) and striploin (longissimus lumborum muscle) during cold storage.

机构信息

Graduate School of International Agricultural Technology, Seoul National University, Pyeongchang 25354, Republic of Korea; Institutes of Green Bio Science and Technology, Seoul National University, Pyeongchang 25354, Republic of Korea.

Department of Animal Science and Technology, Chung-Ang University, Anseong 17546, Republic of Korea.

出版信息

Food Chem. 2021 Feb 15;338:128029. doi: 10.1016/j.foodchem.2020.128029. Epub 2020 Sep 8.

DOI:10.1016/j.foodchem.2020.128029
PMID:32932089
Abstract

Peptides derived from whole proteins in beef tenderloin (M. psoas major, PM) and striploin (M. longissimus lumborum, LL) associated with meat quality and muscle fiber composition were identified and quantified during 21 days of aging. Peptide quantification revealed 40-43 proteins to be significantly degraded during all aging time, and these were mostly sarcoplasmic proteins. Cooking loss of both muscles was not changed by aging (P > 0.05), whereas Warner-Bratzler shear force and meat color were affected by aging. Sensory tenderness increased in PM after 14 days of aging (P < 0.05). PM had a higher type I fiber content, whereas LL had a higher type IIX fiber content (P < 0.05), resulting in differences in proteolysis during all aging periods tested. These findings improve our understanding of different biochemical and physicochemical changes in aged meat according to the muscle type.

摘要

在 21 天的成熟过程中,从牛里脊肉(腰大肌,PM)和牛里脊(腰最长肌,LL)中的完整蛋白质中分离并定量了与肉质和肌肉纤维组成相关的肽。肽定量分析显示,在整个成熟过程中,有 40-43 种蛋白质发生了显著降解,这些蛋白质大多是肌浆蛋白。两种肌肉的蒸煮损失不受成熟(P>0.05)的影响,而 Warner-Bratzler 剪切力和肉色受成熟的影响。PM 的感官嫩度在成熟 14 天后增加(P<0.05)。PM 含有更高的 I 型纤维含量,而 LL 含有更高的 IIX 纤维含量(P<0.05),导致在所有测试的成熟阶段存在不同的蛋白水解。这些发现有助于我们根据肌肉类型了解成熟肉的不同生化和理化变化。

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