کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2435543 | 1107080 | 2008 | 8 صفحه PDF | دانلود رایگان |
A novel approach to α-lactalbumin (α-LA) isolation from sweet whey comprised a membrane filtration and a tryptic treatment of permeate. The ultrafiltration (UF) was performed with a laboratory and a pilot-scale equipment using membranes with 100 and 150 kDa molecular mass cut-off limits, respectively. The transmission of α-La was optimal at 45 °C, 2.0 bar and at pH 6.7. The transmission of proteins was proportional to the volume reduction ratio. Under these conditions, the transmission of α-LA into the permeate was about 25% and the purity was about 36% and 44% (inclusive caseinomacropeptide (CMP)) on the laboratory- and pilot-scale, respectively. For further purification, a tryptic hydrolysis step was applied. At a 10.0% hydrolysis degree, all the β-lactoglobulin was digested and practically no α-LA was degraded, while serum albumin remained in the hydrolysate as the only impurity. If the hydrolysis was prolonged a partial digestion of α-LA was observed. After a second UF and diafiltration of the hydrolysate using a 10 kDa membrane, the calculated overall recoveries were up to 15% of the α-LA present with a purity of 90–95%. The new method was found to be reproducible, selective and robust.
Journal: International Dairy Journal - Volume 18, Issue 1, January 2008, Pages 47–54