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Concentration of a vegetal enzymatic extract by microfiltration

机译:微滤浓度植被酶提取物

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Milk clotting for cheese producing is usually performed using enzymes from animal sources and the most common, chymosin, is obtained from the stomach of newborn calves. Some researches have identified new sources of enzymes that have the ability of coagulating the milk like proteases from vegetal. The objective of this study was to evaluate the concentration by microfiltration of a vegetal proteolytic enzymatic extract obtained from sunflower seed. The raw material utilized was sunflower seed from Embrapa's experimental station. Enzyme extraction was performed according to the following procedure: sunflower seed disintegration in a pilot plant mill, homogenization in an industrial blender and aqueous extraction in brine solution during 18 hours under refrigeration. The extract was centrifuged and conducted to microfiltration system composed by three ceramic membranes with 1.0 μm pore size. Permeate flux was determined along the process and samples were collected from feed, permeate and retentate, for determination of total proteins, proteolytic activity and coagulation unit. Average permeate flux was 33 L/hm~2 and concentration factor was equal to 5.0. As expected the coagulation unit was lower in retentate fraction (4.72 CU/mL) than in feed (10.93 CU/mL) and no milk coagulation was verified with the permeate sample. No proteolytic activity was detected in permeate fraction and total protein content was 0.29 mg/mL. Proteolytic activity increased from 1.43 U/mL in raw extract to 2.18 U/mL in retentate and protein content has increased from 1.69 mg/mL to 6.21 mg/mL. Both total protein and proteolytic activity were concentrated in retentate fraction although they were not in the same range of the concentration factor, probably due to the protein denaturing and loss of enzymatic activity. The obtained results suggest a potentiality for the concentration of the sunflower seed protease by microfiltration, although it is needed further studies to optimize the process.
机译:奶酪生产的牛奶凝结通常使用来自动物来源的酶和最常见的胰蛋白酶从新生犊牛的胃中获得。一些研究已经确定了新的酶来源,其具有与植物的蛋白酶凝结乳的能力。本研究的目的是评价由向日葵种子获得的植物蛋白水解酶提取物的微滤浓度。利用的原料是来自阿布拉帕的实验站的向日葵种子。根据以下步骤进行酶提取:在先导植物磨机中的向日葵种子崩解,在制冷下18小时后盐水溶液中的均质化和盐水溶液中的均质化。将提取物离心并进行到由具有1.0μm孔径的三个陶瓷膜组成的微滤系统。沿着该方法测定渗透通量,并从饲料,渗透物和滞留物中收集样品,用于测定总蛋白质,蛋白水解活性和凝血单元。平均渗透通量33L / hm〜2,浓度因子等于5.0。由于预期,凝结单元在滞留率馏分(4.72u / ml)中低于饲料(10.93u / ml),并且没有用渗透物样品验证牛奶凝结。在渗透物级分中检测蛋白水解活性,总蛋白质含量为0.29mg / ml。蛋白水解活性从1.43 u / ml增加到原萃取物至2.18u / ml,滞留物,蛋白质含量从1.69mg / ml增加到6.21mg / ml。虽然它们不在浓度因子的相同范围内,但它们的浓缩蛋白质和蛋白水解活性均以浓缩的部分浓缩,这可能是由于蛋白质变性和酶活性的损失。所获得的结果表明,通过微滤浓度对向日葵种子蛋白酶浓缩的潜力,尽管需要进一步的研究以优化该过程。

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