食品科学 ›› 2010, Vol. 31 ›› Issue (17): 228-231.doi: 10.7506/spkx1002-6630-201017051

• 生物工程 • 上一篇    下一篇

耐热蛋白酶对UHT乳蛋白水解作用

王 辉1,2,吕加平1,*,刘 鹭1,靳 磊1   

  1. 1.中国农业科学院农产品加工研究所,农业部农产品加工与质量控制重点开放实验室
    2.国家知识产权局专利审查协作中心
  • 收稿日期:2009-12-18 出版日期:2010-09-15 发布日期:2010-12-29
  • 通讯作者: 吕加平 E-mail:liquider@sina.com
  • 基金资助:

    国家科研院所社会公益项目(2002005DIA4G035-7);“十一五”国家科技支撑计划项目(2006BAD04A07;2006BAD04A10)

Hydrolysis Effect of Heat-resistant Protease on UHT Milk

WANG Hui1,2,LU Jia-ping1,*,LIU Lu1,JIN Lei1
(1. Institute of Agro-food Science and Technology, Key Laboratory of Agricultural Product Processing   

  1. 1. Institute of Agro-food Science and Technology, Key Laboratory of Agricultural Product Processing and Quality Control, Ministry of
    Agriculture, Chinese Academy of Agricultural Sciences, Beijing 100193, China;2. Patent Examination Cooperation Center of State
    Intellectual Property Office, Beijing 100190, China
  • Received:2009-12-18 Online:2010-09-15 Published:2010-12-29
  • Contact: LU Jia-ping E-mail:liquider@sina.com

摘要:

采用SDS-PAGE、Urea-PAGE 分析耐热蛋白酶对UHT 乳蛋白的水解作用。结果表明:荧光假单胞菌(PF)蛋白酶和纤溶酶(PL)作用底物不同,产物也不同;前者优先水解κ- 酪蛋白生成副κ- 酪蛋白,而PL 主要水解β- 酪蛋白与α- 酪蛋白生成γ- 酪蛋白及胨、肽等。分别经PL和细菌蛋白酶水解3h的UHT乳水解产物,在pH4.6和12g/100mL三氯乙酸(TCA)沉淀后经反相高效液相色潽仪(RP-HPLC)分析滤液,两者呈现不同的色谱图。

关键词: 耐热蛋白酶, UHT乳, 水解

Abstract:

The effect of heat-resistant protease on protein proteolysis of UHT milk was evaluated by SDS-PAGE and Urea- PAGE. Results indicated that different proteases reacted with different substrates in milk to produce different peptides. Pseudomonas fluorescens protease hydrolyzed κ -casein into para- κ -casein. Plasminogen hydrolyzed α -casein and β -casein into γ-casein, peptone and peptides. In addition, the leftover supernatants after trichloroacetic acid precipitation of the 3 h hydrolysates of UHT milk prepared with plasminogen and bacterial proteases exhibited different RP-HPLC profiles and those of the pH 4.6 soluble peptide in the 3 h hyolroluysates were also different.

Key words: heat-resistant protease, UHT milk, proteolysis

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