Sequential Separation of Lysozyme and Ovalbumin from Chicken Egg White

• 발행기관: 한국축산식품학회
• 저자명: Nalaka Sandun Abeyrathne Hyun Yong Lee Dong Uk Ahn
• 간행물 정보: 『Food Science of Animal Resources』Korean Journal for Food Science of Animal Resources 제33권 제4호, 501~507쪽, 전체 7쪽
• 주제분류: 농수해양 > 식품과학
• 파일형태: PDF
• 발행일자: 2013.08.31

영문 초록

Lysozyme was trapped from 2× diluted egg white using Amberlite FPC 3500 ion exchange resin (1 g/10mL of egg white). The lysozyme bound to the resin was recovered using 0.1 N glycine-NaOH buffers, pH 9.0, containing 0.5 M NaCl. After separating lysozyme, the pH of the egg white solution was adjusted to 4.75 and centrifuged to remove interfering proteins. The supernatant was collected, added with 2.5% citric acid and 5.0% ammonium sulfate combination to precipitate egg white proteins, except for ovalbumin. After centrifugation, both supernatant (S1) and precipitant were collected. The precipitant was dissolved with 4 volumes of distilled water, and then 2.0% ammonium sulfate and 1.5% citric acid combinations added, stirred overnight in a cold room, and centrifuged. The resulting supernatant (S2) was pooled with the first supernatant (S1), desalted using an ultrafiltration unit, heat-treated at 70oC for 15 min, and then centrifuged. The supernatant was collected as an ovalbumin fraction and lyophilized. The separated proteins were confirmed using Western blotting. The yield of lysozyme and ovalbumin was > 88.9% and > 97.7%, respectively, and the purity of lysozyme and ovalbumin was > 97% and 87%, respectively. The results indicated that the protocol was simple, and separated lysozyme and ovalbumin effectively.

키워드

ovalbumin lysozyme ammonium sulfate citric acid egg white sequential separation