[1]鲍俊旺,李越,翁凌,等.凡纳滨对虾多酚氧化酶的纯化及性质分析[J].集美大学学报(自然版),2019,24(2):100-109.
 BAO Junwang,LI Yue,WENG Ling,et al.Purification and Characterization of Polyphenol Oxidase from Pacific White Shrimp Litopenaeus vannamei[J].Journal of Jimei University,2019,24(2):100-109.
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凡纳滨对虾多酚氧化酶的纯化及性质分析()
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《集美大学学报(自然版)》[ISSN:1007-7405/CN:35-1186/N]

卷:
第24卷
期数:
2019年第2期
页码:
100-109
栏目:
水产、食品与生物技术
出版日期:
2019-03-28

文章信息/Info

Title:
Purification and Characterization of Polyphenol Oxidase from Pacific White Shrimp Litopenaeus vannamei
作者:
鲍俊旺1李越1翁凌12张凌晶12孙乐常12曹敏杰12
( 1.集美大学食品与生物工程学院,福建 厦门 361021;2.水产品深加工技术国家地方联合工程研究中心,福建 厦门 361021)
Author(s):
BAO Junwang1LI Yue1WENG Ling12ZHANG Lingjing12SUN Lechang12CAO Minjie12
(1.College of Food and Biological Engineering,Jimei University,Xiamen 361021,China;2.National & Local Joint Engineering Research Center for Aquatic Products Processing,Xiamen 361021,China)
关键词:
凡纳滨对虾多酚氧化酶纯化黑变
Keywords:
Litopenaeus vannameipolyphenol oxidasepurificationmelanosis
文献标志码:
A
摘要:
通过硫酸铵盐析、DEAE-Cellulose离子交换、Phenyl-Sepharose疏水层析、Hi-Trap Capto-Q强阴离子交换层析等方法,从凡纳滨对虾(Litopenaeus vannamei)虾头中分离纯化出一种多酚氧化酶(polyphenol oxidase,PPO),十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate polyacrylamide gel electropheresis,SDS-PAGE)显示其分子质量约为210 ku。肽质量指纹图谱的比对结果表明,纯化得到的PPO中含有187个氨基酸残基的14个片段与NCBI数据库中酚氧化酶原(gi|147724160)序列相似性为100%。该酶的最适温度和最适pH值分别为40 ℃和6.0,且在温度0~50 ℃及pH=5.0~8.0可保持相对稳定的活性。圆二色谱分析结果表明,对虾PPO的二级结构主要为反平行结构及无规则卷曲。抗坏血酸、茶多酚和特丁基对苯二酚(tertiary butylhydroquinone,TBHQ)等具有生物活性羟基的抑制剂对其均有较好的抑制效果。
Abstract:
In this study,a polyphenol oxidase (PPO) was purified to homogeneity from Pacific white shrimp (Litopenaeus vannamei) by ammonium sulfate fractionation and column chromatographies including DEAE-Cellulose,Phenyl-Sepharose HP and Hi-Trap Capto-Q. SDS-PAGE showed that the molecular weight of L.vannamei PPO was about 210 ku and its optimal temperature and pH were 40 ℃ and 6.0,respectively.Comparison of sequences between the purified PPO and prophenol oxidase (gi|147724160) of L.vannamei in the database of NCBI showed a similarity of 100% on 187 amino acid residues of 14 peptide fragments.The activity of PPO remained stable at 0~50 ℃ and in the pH range of 5.0~8.0.The secondary structure of PPO was mainly anti-parallel β-sheet and random coil as revealed by circular dichrosim(CD).Additives of ascorbic acid,tea-polyphenols,and tertiary butylhydroquinone (TBHQ) inhibited the enzyme activity effectively.

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更新日期/Last Update: 2019-05-05