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Isolation of whey protein and hydrolysis pattern of whey protein by proteolytic enzyme

유청단백질의 분리 및 단백질 분해 효소에 의한 유청단백질의 가수분해 양상

  • 렌친핸드 (충남대학교 동물바이오시스템과학과) ;
  • 배형철 (충남대학교 동물바이오시스템과학과) ;
  • 정석근 (농촌진흥청 국립축산과학원 축산물이용과) ;
  • 남명수 (충남대학교 동물바이오시스템과학과)
  • Received : 2012.11.01
  • Accepted : 2012.12.13
  • Published : 2012.12.31

Abstract

The aim of this study was to introduce a simple method for isolation of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin from cow's milk, and peptides produced by enzymatic hydrolysis of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Whey protein were precipitated from whey by ammonium sulfate and, ${\alpha}$-lactalbumin and ${\beta}$-lactoglobulin were isolated using Hi Prep 26/60 Sephacryl S-100 column gel filtration chromatography. Bovine serum albumin and ${\beta}$-lactoglobulin were isolated by Mono-Q 5/50 GL column anion exchange chromatography of the 50% Ammonium Sulfate-supernatant. Isolated whey proteins were hydrolyzed by proteolytic alcalase. Tricine SDS-PAGE and reverse-phase HPLC analyses revealed that almost hydrolyzed all the ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Molecular weight of various peptides derived from alcalase hydrolysate were small molecular weight than 3.5 kDa.

Keywords

References

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