干热处理对杏鲍菇蛋白质功能和结构的影响  

Effect of Dry Heat Treatment on the Function and Structure of Pleurotus eryngii Protein

作　　者：陈怡静 李萍 康雨薇 高璐[1] 王琨 崔桂友[1] 许慧卿[1] CHEN Yi-jing;LI Ping;KANG Yu-wei;GAO Lu;WANG Kun;CUI Gui-you;XU Hui-qing(College of Food Science and Engineering,Yangzhou University,Yangzhou 225127,Jiangsu,China;Culinary Science and Technology College,Jiangsu College of Tourism,Yangzhou 225500,Jiangsu,China;Jiangsu Konen Biologineering Company Limited,Yizheng 211413,Jiangsu,China)

机构地区：[1]扬州大学食品科学与工程学院,江苏扬州225127 [2]江苏旅游职业学院烹饪科技学院,江苏扬州225500 [3]江苏康能生物工程股份有限公司,江苏仪征211413

出　　处：《食品研究与开发》2022年第19期103-108,共6页Food Research and Development

摘　　要：该文研究不同干热处理温度对杏鲍菇蛋白质功能和结构的影响。将杏鲍菇分离蛋白经65、80、95、110、125℃干热处理30 min。通过电镜观察发现干热处理后的蛋白质表面出现裂纹和小孔。总巯基组和游离巯基组相较于未经干热处理杏鲍菇蛋白质显著(p<0.05)降低。干热处理后杏鲍菇蛋白质的溶解度得到提高。随着干热处理温度的升高,杏鲍菇蛋白质的发泡能力在95℃时达到最高,但其稳定性却不如未处理的生样蛋白。圆二色性光谱和紫外光谱显示杏鲍菇蛋白二级结构和三级结构发生变化,二级结构被破坏程度增加,但三级结构在110℃和125℃两组蛋白质的吸光度低于未处理组,这可能是由于温度的升高使展开的小分子发生聚集形成大分子。总体而言,经过干热处理蛋白质的结构发生改变,在95℃加热30 min时,杏鲍菇蛋白质的功能特性达到较高水平。The function and structure of Pleurotus eryngii protein under different dry heat treatments temperatures were studied.The isolated proteinsamples were exposed to the air at 65,80,95,110℃and 125℃,respectively,for 30 min.Cracks and small pores were observed on the surface of the treated protein under an electron microscope.The total sulfhydryl groups and free sulfhydryl groups in the dry heated protein reduced(p<0.05)compared with those of the no dry heat protein.The solubility of the protein was improved after dry heat treatment.With the increase in temperature,the foaming ability of the protein increased andpeaked at 95℃,while the treated protein was less stable than the untreated protein.Circular dichroism spectra and UV spectra showed changes in the secondary and tertiary structures of P.eryngii protein.The secondary structure was increasingly disrupted with the increase in temperature,while the tertiary structure of the protein treated at 110℃and 125℃showcased lower absorbance than that of the untreated protein,which might be because the increased temperature made the unfolded small molecules aggregate to form large molecules.Overall,dry heat treatment changed the structure of P.eryngii protein,and the protein heated at 95℃for 30 min demonstrated the best functional properties.

关 键 词：杏鲍菇蛋白 干热处理 温度 功能特性 结构 

分 类 号：TS219[轻工技术与工程—粮食、油脂及植物蛋白工程]