열처리로 야기되는 우유 유청 단백질의 반응

• 발행기관: 한국축산식품학회
• 저자명: 이유라 홍윤호
• 간행물 정보: 『Food Science of Animal Resources』Korean Journal for Food Science of Animal Resources 제22권 제2호, 179~182쪽, 전체 4쪽
• 주제분류: 농수해양 > 식품과학
• 파일형태: PDF
• 발행일자: 2002.06.30

영문 초록

Using differential scanning calorimetry (DSC), changes underwent by a mixture of α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) during heat treatment were studied, yielding useful information for the dairy industry. Rusults of the DSC showed that the heat denaturation temperature of the holo-α-La was higher than that of apo-α-La, suggesting holo-α-La`s greater stability. The denaturation temperature of a mixture of holo-α-La and β-Lg was also slightly lower than that of holo-α-La alone. The denaturation temperature of an apo-α-La and β-Lg mixture was higher than that of holo-α-La and β-Lg, suggesting that the heat stability of apo-α-La was increased by β-Lg. Based on these results, it is possible to conclude that a mixture of holo-α-La and β-Lg is more inensively affected by an increase in temperature than other samples, and that free sulphydryl groups seem to take part in this heat-induced denaturation.