Binding affinity of proanthocyanidin from waste Pinus radiata bark onto proline-rich bovine achilles tendon collagen type I

被引:90
作者
Ku, C. S.
Sathishkumar, M. [1 ]
Mun, S. P.
机构
[1] Chonbuk Natl Univ, Coll Agr & Life Sci, Dept Food Sci & Technol, Jeonju 561756, South Korea
[2] Chonbuk Natl Univ, Dept Adv Organ Mat Engn, Jeonju 561756, South Korea
[3] Chonbuk Natl Univ, Coll Agr & Life Sci, Div Forest Sci, Jeonju 561756, South Korea
关键词
Pinus radiata; waste bark; proanthocyanidin; collagen; adsorption;
D O I
10.1016/j.chemosphere.2006.11.037
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
Binding affinity of proanthocyanidin (PA) purified from Pinus radiata bark waste onto bovine Achilles tendon collagen (type I) was studied. Adsorption of PA onto the collagen was optimized by examining pH, contact time and temperature. The adsorption was pH-dependent. The maximum adsorption capacity (Q(0)) of PA on collagen was found to be 211 mg g(-1) using the Langmuir isotherm. Comparison between two adsorbents also showed that collagen had higher adsorptivity of approximately 20% more than PVPP (polyvinyl polypyrrolidone). The high affinity between PA and collagen was further confirmed in solvent solubility experiments. The observed solvent resistance was thought to be mainly due to a hydrophobic stacking mechanism reinforced by hydrogen bonding. FT-IR spectra clearly indicated the presence of PA adsorbed on collagen. The results have interesting implications that PA can be a good protective agent for collagen against collagenase and other enzymes. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1618 / 1627
页数:10
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