Autolysis and Characterization of Sarcoplasmic and Myofibril Associated Proteinases of Oxeye Scad (Selar boops) Muscle
Autolysis and Characterization of Sarcoplasmic and Myofibril Associated Proteinases of Oxeye Scad (Selar boops) Muscle
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DOI：
10.1080/10498850.2015.1032462
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发表时间：
2016-01-01
影响因子：
1.6
通讯作者：
Benjakul, Soottawat
中科院分区：
文献类型：
--
作者：
Wongwichian, Chantira;Chaijan, Manat;Benjakul, Soottawat
研究了牛眼鳞片的自溶特征。肉糜的蛋白水解活性高于水洗肉糜。肉糜和洗净肉糜分别在65℃和60℃时自溶最高。肉糜和水洗肉糜的最适自溶pH均为9.0，随着NaCl浓度的增加（0 ~ 3.5%），活性逐渐降低。大豆胰蛋白酶抑制剂（SBTI）能明显抑制洗净肉糜的自溶，提示肌原纤维相关蛋白酶为丝氨酸蛋白酶。肌浆蛋白酶为热活化碱性蛋白酶，最适pH为9.0℃，最适温度为60℃。在20 ~ 40℃pH 8.0 ~ 11.0范围内活性稳定，粗蛋白酶被n -对-赖氨酸氯甲基酮、SBTI和苯基甲基磺酰氟抑制，表明丝氨酸蛋白酶占优势，尤其是胰蛋白酶。NaCl抑制其活性，-巯基乙醇、二硫苏糖醇和CaCl2使其活性增强。因此，胰蛋白酶样蛋白酶是牛眼烫伤肌肉自溶的主要内源性蛋白酶。本研究结果可作为预测牛眼鳞片鱼糜凝胶强度的科学依据。
The autolytic profile of oxeye scad mince was characterized. Mince showed higher proteolytic activity than washed mince. The highest autolysis was observed at 65 and 60 degrees C for mince and washed mince, respectively. Both mince and washed mince showed the optimum pH for autolysis at pH 9.0, and their activities decreased with increasing NaCl concentration (0-3.5%). Autolysis of washed mince was markedly inhibited by soybean trypsin inhibitor (SBTI), suggesting that myofibril-associated proteinase was serine proteinase. Sarcoplasmic proteinase was characterized to be heat-activated alkaline proteinase having the optimal pH and temperature of 9.0 and 60 degrees C, respectively. The activities were stable at pH range of 8.0-11.0 at 20-40 degrees C. The crude proteinase was inhibited by N-p-tosyl-L-lysine chloromethyl ketone, SBTI, and phenylmethanesulfonyl fluoride, suggesting the predominance of serine proteinases, especially trypsin. NaCl suppressed the activity while -mercaptoethanol, dithiothreitol, and CaCl2 activated the activity. Therefore, trypsin-like proteinase is a major endogenous proteinase responsible for autolysis in oxeye scad muscle. The present results can be used as scientific guidelines to predict the gel strength of surimi made from oxeye scad muscle.