研究报告

不同产蛋白酶乳酸菌对风干牛肉蛋白质氧化的影响

  • 刘世琳 ,
  • 李宇辉 ,
  • 王俊钢 ,
  • 卢士玲 ,
  • 李晓楠 ,
  • 李蕊婷 ,
  • 岳建平
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  • 1(石河子大学 食品学院,新疆 石河子,832000)
    2(新疆农垦科学院,农产品加工研究所,新疆 石河子,832000)
    3(新疆农垦科学院,农产品加工重点实验室,新疆 石河子,832000)
    4(额敏县新大同创生物工程有限责任公司,新疆 额敏,834699)
硕士研究生(王俊钢副研究员和卢士玲教授为共同通讯作者,E-mail:wjgang728@126.com;lushiling_76@163.com)

收稿日期: 2021-02-07

  修回日期: 2021-03-10

  网络出版日期: 2021-11-18

基金资助

国家自然科学基金地区科学基金(31860437);新疆生产建设兵团中青年领军人才项目(2020CB024)

Effects of different protease-producing lactic acid bacteria on the oxidation of air-dried beef protein

  • LIU Shilin ,
  • LI Yuhui ,
  • WANG Jungang ,
  • LU Shiling ,
  • LI Xiaonan ,
  • LI Ruiting ,
  • YUE Jianping
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  • 1(College of Food Science and Technology, Shihezi University, Shihezi 832000, China)
    2(Institute of Agro-products Processing Science and Technology, Xinjiang Academy of Agricultural and Reclamation Science, Shihezi 832000, China)
    3(Key Laboratory of Agro-Products Processing, Xinjiang Academy of Agricultural and Reclamation Science, Shihezi 832000, China)
    4(Emin County Xinda Tongchuang Biological Engineering Limited Liability Company, Emin 834699, China)

Received date: 2021-02-07

  Revised date: 2021-03-10

  Online published: 2021-11-18

摘要

为明确产蛋白酶乳酸菌在风干牛肉制作过程中对牛肉蛋白质氧化的影响,以牛后腿肉为研究对象,通过分别接种3株产蛋白酶能力较高的乳酸菌:乳酸乳球菌(S-1)、格式乳球菌(S-2)、戊糖片球菌(S-3)制备风干牛肉,以不添加发酵剂的样品为对照组(CK),运用化学法和拉曼光谱技术分析风干肉制作过程中牛肉肌原纤维蛋白分子结构变化。结果表明,随着加工时间的延长,牛肉蛋白中离子键和氢键含量显著下降(P<0.05),疏水相互作用和二硫键含量显著升高(P<0.05)。与对照组相比,乳酸乳球菌(S-1)组蛋白质羰基含量和蛋白质表面疏水性显著降低(P<0.05);格式乳球菌(S-2)的总巯基含量显著高于对照组(P<0.05);与对照组相比,添加产蛋白酶乳酸菌明显降低了肌原纤维蛋白的β-折叠含量(P<0.05)。综上,产蛋白酶乳酸菌处理能够显著改变牛肉蛋白质的化学作用力及肌原纤维蛋白的结构,其中,乳酸乳球菌(S-1)有潜力成为风干牛肉中的抗氧化发酵剂。

本文引用格式

刘世琳 , 李宇辉 , 王俊钢 , 卢士玲 , 李晓楠 , 李蕊婷 , 岳建平 . 不同产蛋白酶乳酸菌对风干牛肉蛋白质氧化的影响[J]. 食品与发酵工业, 2021 , 47(20) : 68 -74 . DOI: 10.13995/j.cnki.11-1802/ts.026948

Abstract

In order to determine the effect of protease-producing lactic acid bacteria(LAB) on the protein oxidation in air-dried beef, three LAB strains with high protease-producing ability were inoculated, namely Lactococcus lactis (S-1), Lactococcus gracilis (S-2) and Pediococcus pentosaceus (S-3). The chemical method and Raman spectroscopy were used to analyze the molecular structure of beef myofibrin during the preparation of dried meat. The results showed that the content of ionic bond and hydrogen bond in beef protein decreased significantly(P<0.05), while the hydrophobic interaction and disulfide bond content increased significantly(P<0.05). Compared with the control group, carbonyl and surface hydrophobicity in protein of S-1 group were significantly decreased (P<0.05), the content of sulfhydryl group in S-2 group increased significantly(P<0.05). Furthermore, the addition of protease-producing LAB significantly reduced the β-sheet content of myofibril protein (P<0.05). Therefore, LAB proteases can significantly change the chemical action of beef protein and the structure of myofibrin, and Lactococcus lactide(S-1) has the potential to be an antioxidant starter in air-dried beef.

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