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当前位置: 首页 > 文章 > 酶法提取猪皮胶原及产物性质分析 食品科学 2013,34 (19) 123-127
Position: Home > Articles > Enzymatic Extraction and Characterization of Collagens from Pigskin FOOD SCIENCE 2013,34 (19) 123-127

酶法提取猪皮胶原及产物性质分析

作  者：
张玲;芮汉明;张立彦
单  位：
华南理工大学轻工与食品学院;广东石油化工学院化学与生命科学学院
关键词：
猪皮;胶原;提取;性质
摘  要：
以新鲜猪背脊皮为原料,采用超声波介入原料脱脂预处理、低温酶法提取分离猪皮胶原,测定胶原产物的纯度、等电点、分子质量分布、热变性温度及氨基酸组成,并对其进行紫外及红外分析。结果表明:采用超声波介入鲜猪皮脱脂不但提高了脱脂效果,而且对胶原产物的天然结构不会造成负面影响;提取胶原的理想工艺为:用经过超声波脱脂预处理的猪皮为原料,选用酶活力为3000U/mg的胃蛋白酶,酶用量为1:50(m/m),料液比为1:10(m/V),于pH2.5、4℃提取24h;产物的紫外最大吸收在225nm波长处,符合胶原特征;纯度为95.7%;等电点约为4.91;热变性温度约为38℃;数均分子质量为4.81×103g/mol,重均分子质量为2.57×105g/mol,分布较为集中且呈连续分布状态;产物氨基酸组成非常符合胶原的一级结构特征。
译  名：
Enzymatic Extraction and Characterization of Collagens from Pigskin
作  者：
ZHANG Ling;RUI Han-ming;ZHANG Li-yan;College of Chemistry and Life Science,Guangdong University of Petrochemical Technology;College of Light Industry and Food Sciences,South China University of Technology;
关键词：
pigskin;;collagen;;extraction;;characterization
摘  要：
This study aimed to optimize the extraction conditions of collagens from fresh back pigshin by ultrasonicassisted and enzymatic hydrolysis at a low temperature. The collagen was characterized by analyzing its purity, isoelectric point, molecular weight distribution, thermal denaturation temperature and amino acid composition. FTIR and UV spectral properties were analyzed as well. The results showed that ultrasonic-assisted extraction was favorable to defatting of pigskin without any negative impact on the natural structure of collagen. The optimal extraction conditions were obtained as follows: material/liquid ratio 1:10(m/V), pepsin dosage 1:50(m/m), pH 2.5, extraction time 24 hours and extraction temperature 4 ℃. The maximum absorption wavelength of the extract was 225 nm, consistent with the characteristics of collagen. The purity and isoelectric point was 95.7% and 4.91, respectively. The thermal denaturing temperature was around 38 ℃. The number-average molecular weight was 4.81 × 103 g/mol while the weight-average molecular weight was 2.57 × 105 g/mol, indicating a concentrated and continuous distribution. Its amino acid composition complied with the primary structure of collagen.

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