珍珠贝肉蛋白酶解过程浑浊形成机理研究  

Research on Turbid Formational Mechanism of Pearl Oyster Protein During Hydrolysis

作　　者：吴胜旭[1] 赵谋明[1] 崔春[1] 章超桦[2] 

机构地区：[1]华南理工大学轻工与食品学院,广东广州510640 [2]广东海洋大学食品科技学院,广东湛江524088

出　　处：《食品与发酵工业》2009年第2期27-30,34,共5页Food and Fermentation Industries

基　　金：农业部“948”项目(2006-G42);粤港招标突破项目(2007A020901001)

摘　　要：以浑浊度为指标,研究不同酶解时间珍珠贝肉蛋白酶解液浑浊度与粒度分布之间的联系,结果表明,二者呈正相关关系(R2=0.91);而凝胶渗透色谱表明酶解3h大部分蛋白质被降解成小分子肽,粒度分布结果显示酶解体系中粒度从383.9nm快速增加到801.4nm,氨基酸分析结果表明此过程中肽基疏水性氨基酸含量从0h的22.29%上升到3h的28.79%,而表面疏水性从559.69下降至3h的138.96,二硫键数目维持在470μmol/g,这证明了浑浊物是在酶解初期由肽凝集形成的,疏水相互作用在浑浊物形成过程中起重要作用。In this paper, using turbidity as a meter, we study the correlation between turbidity and particle distribution of the pearl oyster protein hydrolysate at different times, the result implies a positive relationship between them（R^2 =0.91）. Gel Permeation Chromatograph Scanning spectra show protein is degraded into peptides in the first 3 hours. The particle distribution analysis of hydrolysate shows the particle sizes increase from 383.9nm to 801.4nm. The amino acids analysis indicates the hydrophobic amino acids content of peptides also increases from 22.29% to 28. 79%, the surface hydrophobicity decreases from 559.69 to 138.96 in the first 3 hours, the content of disulfide bond remains at 470μmol/g till the hydrolysis terminal, showing that the turbid is formed by the peptides through aggregation in the beginning hydrolysis stage, and hydrophobic interaction plays an important part during the turbid formation.

关 键 词：浑浊 粒度分布 表面疏水性 二硫键 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]