摘要
以糙米为原料,建立利用低浓度氢氧化钠从稻米胚乳中分离蛋白体的方法。以蛋白体体积分数为指标,得到蛋白体分离条件为:碱液浓度14 mmol/L、液料比12 mL/g、搅拌时间90 min、超声功率90 W、超声温度35℃和超声时间40 min,蛋白体体积分数达20.10%。再经0.1、5.0μm滤膜过滤及4.0 mol/L氯化钙去除残余淀粉,获得纯化的蛋白体。所得蛋白体呈微球形,有荧光;具有16、22、33、57 ku的蛋白亚基;X-衍射19.9°处显示β-折叠峰;红外1464、1534 cm^(-1)属于AmideⅡ带;拉曼1303、1651 cm^(-1)属于AmideⅢ和AmideⅠ带,均为蛋白质的特征吸收。因此,以低浓度氢氧化钠分离并经微孔滤膜和氯化钙纯化从稻米中获取蛋白体是可行的,这为研究稻米胚乳中蛋白体的结构和性质提供了方法学参考。
Brown rice was used as the raw material,a method of separating protein bodies from rice endosperm with low concentration of sodium hydroxide was established.With the volume fraction of protein body as the index,the separation conditions of protein body were obtained as follows:alkali concentration of 14 mmol/L,liquid-to-material ratio of 12 mL/g,stirring time of 90 min,ultrasonic power of 90 W,ultrasonic temperature of 35℃and ultrasonic time of 40 min,and the volume fraction of protein body reached 20.10%.After another 0.1μm and 5.0μm membrane filtration and 4.0 mol/L calcium chloride were used to remove residual starch to obtain purified protein bodies.The obtained protein body was microsphere with fluorescence.It had protein subunits of 16,22,33,57 ku;X-ray diffraction at 19.9°showedβ-folding peak;infrared peaked at 1464 cm^(-1) and 1534 cm^(-1),being AmideⅡband;Raman 1303 cm^(-1) and 1651 cm^(-1) were AmideⅢand AmideⅠbands,being the characteristic absorption of proteins.Therefore,it was feasible to obtain protein bodies from rice by low concentration sodium hydroxide separation and purification through microporous filtration membrane and calcium chloride,providing a methodological references for studying the structure and properties of protein bodies in rice endosperm.
作者
许子鑫
郭玉宝
魏秦
刘昕煜
王馨雨
Xu Zixin;Guo Yubao;Wei Qin;Liu Xinyu;Wang Xinyu(School of Biological and Food Engineering,Anhui Polytechnic University,Wuhu 241000)
出处
《中国粮油学报》
CAS
CSCD
北大核心
2024年第2期54-62,共9页
Journal of the Chinese Cereals and Oils Association
基金
国家自然科学基金项目(31671784)。
关键词
稻米
蛋白体
分离纯化
形态
结构
鉴定
rice
protein body
isolation and purification
morphology
structure
identification
