Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Antioxidant Activity of Low Molecular Peptides Derived from Milk Protein

유단백질 가수분해에 의해 생성된 저분자 Peptides의 항산화 활성

  • Woo, Sung-Ho (Department of Animal Products and Food Science, Kangwon National University) ;
  • Jhoo, Jin-Woo (Department of Animal Products and Food Science, Kangwon National University) ;
  • Kim, Gur-Yoo (Department of Animal Products and Food Science, Kangwon National University)
  • 우성호 (강원대학교 동물생명과학대학 동물식품응용과학과) ;
  • 주진우 (강원대학교 동물생명과학대학 동물식품응용과학과) ;
  • 김거유 (강원대학교 동물생명과학대학 동물식품응용과학과)
  • Published : 2009.10.31
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Abstract

The principal objective of the current study was to prepare low molecular weight peptides from milk proteins using enzymatic hydrolysis techniques, in an effort to assess the antioxidant activity of these peptides. The casein and whey proteins isolated from fresh milk were treated with several proteolytic enzymes, such as chymotrypsin, pepsin, and trypsin and the resulting low molecular weight peptides were collected by TCA precipitation. Their identity was confirmed by SDS-PAGE analysis. The hydrolysis experiments indicated that whey protein treated with chymotrypsin displayed the highest degree of protein hydrolysis. The antioxidant activity of milk protein hydrolysates was determined by measuring the ABTS-radical scavenging activity. The results of these experiments showed that hydrolysis of the milk protein was effective in increasing their antioxidant activities. Especially, the tryptic digested casein displayed the highest radical scavenging activity (80.7%). The hydrolyzed low molecular weight milk protein was isolated using an ultrafiltration membrane. The casein hydrolysate passed through a membrane with molecular weight cut-off (MWCO) of 3 kDa displayed the strongest antioxidant activity.

본 연구는 유단백질에 단백질 분해효소를 처리하여 가수분해 후 저분자 peptide를 ABTS법을 이용하여 항산화 활성을 측정하여 유단백질 유래 저분자 peptide의 항산화력을 측정하고자 하였다. Chymotrypsin 처리한 유청단백질의 가수분해도가 가장 높았으며, 유청단백질의 락트알부민 및 락토글로브린이 분해되어 분자량 20 kDa 이하의 저분자 단백질이 생성된 것을 전기영동을 통하여 확인하였다. 유단백질의 농도에 따른 항산화 활성을 측정한 결과, 카제인의 항산화 활성이 유청단백질보다 높게 나타났다. 유단백질을 효소에 의하여 가수분해 시 항산화 활성이 증가하였으며, 카제인 가수분해물이 유청단백질 가수분해물과 비교하여 항산화 활성이 더 높았으나, 가수분해도와 항산화 활성도의 관계는 일치하지 않았다. Trypsin에 의한 카제인 가수분해 물의 항산화 활성이 80.7%로 가장 높았다. 본 연구에서는 chymotrypsin과 trypsin에 의한 분자량 3 kDa의 카제인 분획물의 항산화 활성이 가장 우수 하였으며, 유청단백질을 trypsin으로 분해하였을 때 항산화 활성이 증가하였다.

Keywords

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