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Physicochemical Properties and Biological Activities of Collagens with Different Molecular Weights from Alaska Pollack (Theragra chalcogramma) Skin

명태 껍질 유래 콜라겐의 분자량에 따른 이화학적 특성 및 생리활성

  • Yang, Su-Jin (Department of Food Science and Technology, Catholic University of Daegu) ;
  • Hong, Joo-Heon (Department of Food Science and Technology, Catholic University of Daegu)
  • 양수진 (대구가톨릭대학교 식품공학전공) ;
  • 홍주헌 (대구가톨릭대학교 식품공학전공)
  • Received : 2014.06.02
  • Accepted : 2014.07.24
  • Published : 2014.10.31

Abstract

This study was conducted to investigate the physicochemical properties and biological activities of collagens with different molecular weights from Alaska pollack (Theragra chalcogramma) skin as well as their efficacies as functional materials. The molecular weights of collagens were between 1~10 kDa (below 1 kDa (AP1), 1~3 kDa (AP2), 3~10 kDa (AP3), and above 10 kDa (AP4). The protein content of AP4 (40.19 g/100 g) was the highest. Collagen contents of AP1, AP2, AP3, and AP4 were 36.43, 32.23, 19.23, and 14.89%, respectively. The free amino acid and essential amino acid contents of AP1 were higher than those of AP2, AP3, and AP4. Fourier transform infrared spectroscopy spectra of collagens with different molecular weights showed wavenumbers representing the regions of amide I, amide II, amide III, and amide A, respectively. The electron-donating ability (29.51%) and SOD-like activity (38.45%) of AP1 were higher than those of AP2, AP3, and AP4. Tyrosinase inhibition activity of AP1 improved with higher treatment concentration. The rate of inhibition of MMP-1 production in HS68 cells exposed to UVB was suppressed by treatment with AP1 (29.78%) and AP2 (26.49%) at 1 mg/mL. Furthermore, there was a strong correlation between DPPH, superoxide dismutase, tyrosinase activity, and MMP-1 inhibition rate of collagens with different molecular weights.

Acknowledgement

Supported by : 산업통상자원부

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