Journal
CHEMOSPHERE
Volume 67, Issue 8, Pages 1618-1627Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.chemosphere.2006.11.037
Keywords
Pinus radiata; waste bark; proanthocyanidin; collagen; adsorption
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Funding
- Agriculture & Forestry Technology Management Center, Republic of Korea [arpc204102-3] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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.
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