KSBB Journal

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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Investigation of Acyl Chain Specificity of Lipase-OF 360,000 on the Hydrolysis of Fish Oil

물고기 기름의 가수분해에 대한 리파제 Lipase-OF 360,000의 아실체인 특이성 규명

  • Park Ji-suk (Department of Biological engineering, Inha University) ;
  • Kim Han-Ok (Department of Biological engineering, Inha University) ;
  • Kho Hye-won (Department of Biological engineering, Inha University) ;
  • Hur Byung-Ki (Department of Biological engineering, Inha University)
  • 박지숙 (인하대학교 공과대학 생물공학과) ;
  • 김한옥 (인하대학교 공과대학 생물공학과) ;
  • 고혜원 (인하대학교 공과대학 생물공학과) ;
  • 허병기 (인하대학교 공과대학 생물공학과)
  • Published : 2004.12.01
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Abstract

The hydrolysis characteristics of various fatty acids composing the fish oil was investigated for function of acyl chain specificities using Lipase-OF 360,000 from Candida cylindracea. The hydrolysis of fatty acids decreased with the increase of the number of carbon and double bond in the fatty acids, in case that the number of double bond and the position of the first double bond from the methyl group of fatty acids were the same. The position of the first double bond was found to be an acyl chain specificity of Lipase-OF 360,000 for the hydrolysis of fish oil. Lipase-OF 360,000 also showed the another acyl chain specificity that the increase of double bond of fatty acids, having the same number of carbon and the position of double bond, brought about the decrease of hydrolysis.

Candida cylindracea 유래의 Lipase-OF 360,000를 사용하여 물고기 기름을 구성하고 있는 여러 종류의 지방산의 아실 체인 특성과 가수분해율 사이의 함수관계를 규명하였다. 이중결합수와 이중결합이 시작되는 위치, 즉 (n-3), (n-7) 및 (n-9)이 동일할 경우, Lipase-OF 360,000에 의한 지방산의 가수분해율은 지방산을 구성하고 있는 탄소수의 증가에 따라 가수분해율이 감소하는 아실체인 특이성을 나타내었다. 이중결합이 시작되는 탄소의 위치 또한 Lipase-OF 360,000의 가수분해 특이성에 영향을 끼쳤다. 이 외에 Lipase-OF 360,000은 지방산의 탄소수와 이중결합이 시작되는 위치가 동일할 경우, 이중결합수가 증가하면 가수분해율이 감소하는 아실 체인 특이성도 나타내었다. 또한 본 연구에서는 물고기 기름을 구성하고 있는 각 지방산의 가수분해율을 시간의 함수로 제시함으로서 원하는 지방산을 미반응 글리세라이드 혼합물 내로 농축시키는 공정개발의 기초 자료로 활용할 수 있도록 하였다.

Keywords

References

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