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      KCI등재

      실크 피브로인 수화 겔의 형성에 미치는 티로시나아제 및 폴리페놀 화합물의 영향 = Effect of Tyrosinase and Polyphenol Compounds on Hydrogelation of Silk Fibroin

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      https://www.riss.kr/link?id=A101372894

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      다국어 초록 (Multilingual Abstract)

      The formation of silk fibroin (SF) hydrogel can be adjusted by changing physical conditions such as concentration of SF aqueous solution, temperature, pH and salts. In this study, tyrosinase (Tyr), which is an enzyme catalyzing the oxidation of phenol...

      The formation of silk fibroin (SF) hydrogel can be adjusted by changing physical conditions such as concentration of SF aqueous solution, temperature, pH and salts. In this study, tyrosinase (Tyr), which is an enzyme catalyzing the oxidation of phenols such as tyrosine, was used to decrease the gelation time of SF aqueous solution under a fixed conditions. Tyr oxidizes a broad range of phenols into very reactive o-quinones, and consequently quinones undergo non-enzymatic reactions with various nucleophiles. So it is expected that the gelation time of SF aqueous solution could be decreased by polyphenol compound such as caffeic acid and chlorogenic acid. The color of SF aqueous solutions containing Tyr was changed into deeper yellow with Tyr concentration, and also the gelation time of SF aqueous solution slightly decreased. However, the effect of Tyr concentration on gelation time of SF aqueous solution was not significant due to the locational hindrance of tyrosyl residues in SF. Absorbance at 550 nm also showed conformational transition (random coil to $\beta$-sheet conformation) of SF structure. When polyphenol compounds were added into SF/Tyr aqueous solution, the gelation time slightly decreased. However, the phase separation occurred when polyphenol compounds more than 5 mM were added. The results obtained in this study indicate that enzyme and additives have a potential to regulate the gelation behavior of SF aqueous solution, to some extent.

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      참고문헌 (Reference)

      1 A. S. Ferrer, "Tyrosinase : A Comprehensive Review of Its Mechanism" 1247 : 1-11, 1995

      2 U. J. Kim, "Structure and Properties of Silk Hydrogels" 5 : 786-792, 2004

      3 T. Asakura, "Structural Role of Tyrosine in Bombyx mori S ilk Fibroin, Studied by Solid-state NMR and Molecular Mechanics on Peptide Prepared as Silk I and II" 42 : 258-266, 2004

      4 C. Vepari, "Silk as a Biomaterial" 32 : 991-1007, 2007

      5 C. W. G. van Gelder, "Sequence and Structural Features of Plant and Fungal Tyrosinases" 45 : 1309-1323, 1997

      6 M. Yu, "Role of l-3,4- Dihydroxyphenylalanine in Mussel Adhesive Proteins" 121 : 5825-5826, 1999

      7 B. M. Min, "Regenerated Silk Fibroin Nanofibers: Water Vapor-Induced Structural Changes and Their Effects on the Behavior of Normal Human Cells" 6 : 285-292, 2006

      8 P. Monti, "Raman Spectroscopic Characterization of Bombyx mori Silk Fibroin: Raman Spectrum of Silk I" 32 : 103-107, 2001

      9 V. S. Nithianandam, "Quinone-amine Polymers: 18. A Novel Method for the Synthesis of Poly(alkyl aminoquinone)s" 39 : 4095-4098, 1998

      10 B. S. Aytar, "Preparation of Cross-linked Tyrosinase Aggregates" 43 : 125-131, 2008

      1 A. S. Ferrer, "Tyrosinase : A Comprehensive Review of Its Mechanism" 1247 : 1-11, 1995

      2 U. J. Kim, "Structure and Properties of Silk Hydrogels" 5 : 786-792, 2004

      3 T. Asakura, "Structural Role of Tyrosine in Bombyx mori S ilk Fibroin, Studied by Solid-state NMR and Molecular Mechanics on Peptide Prepared as Silk I and II" 42 : 258-266, 2004

      4 C. Vepari, "Silk as a Biomaterial" 32 : 991-1007, 2007

      5 C. W. G. van Gelder, "Sequence and Structural Features of Plant and Fungal Tyrosinases" 45 : 1309-1323, 1997

      6 M. Yu, "Role of l-3,4- Dihydroxyphenylalanine in Mussel Adhesive Proteins" 121 : 5825-5826, 1999

      7 B. M. Min, "Regenerated Silk Fibroin Nanofibers: Water Vapor-Induced Structural Changes and Their Effects on the Behavior of Normal Human Cells" 6 : 285-292, 2006

      8 P. Monti, "Raman Spectroscopic Characterization of Bombyx mori Silk Fibroin: Raman Spectrum of Silk I" 32 : 103-107, 2001

      9 V. S. Nithianandam, "Quinone-amine Polymers: 18. A Novel Method for the Synthesis of Poly(alkyl aminoquinone)s" 39 : 4095-4098, 1998

      10 B. S. Aytar, "Preparation of Cross-linked Tyrosinase Aggregates" 43 : 125-131, 2008

      11 R. Nazarov, "Porous 3-D Scaffolds from Regenerated Silk Fibroin" 5 : 718-726, 2004

      12 S. Y. Seo, "Mushroom Tyrosinase: Recent Prospects" 51 : 2837-2853, 2003

      13 R. Valluzzi, "Methionine Redox Controlled Crystallization of Biosynthetic Silk Spidroin" 103 : 11382-11392, 1999

      14 H. J. Jin, "Mechanism of Silk Processing in Insects and Spiders" 424 : 1057-1061, 2003

      15 A. Matsumoto, "Mechanism of Silk Fibroin Sol-Gel Transitions" 110 : 21630-21638, 2006

      16 H. Yamamoto, "Insolubilizing and Adhesive Studies of Water-soluble Synthetic Model Proteins" 12 : 305-310, 1990

      17 J. H. Whang, "Inhibitory Effects of Plant Extracts on Tyrosinase, L-DOPA Oxidation, and Melanin Synthesis" 70 : 393-407, 2007

      18 T. Chen, "In Vitro Protein-polysaccharide Conjugation: Tyrosinasecatalyzed Conjugation of Gelatin and Chitosan" 64 : 292-302, 2002

      19 K. Y. Lee, "Hydrogels for Tissue Engineering" 101 : 1869-1879, 2001

      20 G. Wang, "Highly Sensitive Sensors Based on the Immobilization of Tyrosinase in Chitosan" 57 : 33-38, 2002

      21 T. Kameda, "Dynamics of the Tyrosine Side Chain in Bombyx mori and Samia cynthia ricini Silk Fibroin Studied by Solid State 2H NMR" 32 : 8491-8495, 1999

      22 G. D. Kang, "Crosslinking Reaction of Phenolic Side Chains in Silk Fibroin by Tyrosinase" 5 : 234-238, 2004

      23 J. A. Gerrard, "Covalent Protein Adduct Formation and Protein Cross-linking Resulting from the Maillard Reaction between Cyclotene and a Model Food Protein" 47 : 1183-1188, 1999

      24 X. G. Li, "Conformational Transition and Liquid Crystalline State of Regenerated Silk Fibroin" 88 : 497-505, 2008

      25 M. Y. Moridani, "Caffeic Acid, Chlorogenic Acid, and Dihydrocaffeic Acid Metabolism: Glutathione Conjugate Formation" 29 : 1432-1439, 2001

      26 I. Gulcin, "Antioxidant Activity of Caffeic Acid (3,4- dihydroxycinnamic acid)" 217 : 213-220, 2006

      27 K. Komori, "Activity Regulation of Tyrosinase by Using Photoisomerizable Inhibitors" 108 : 11-16, 2004

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      연월일 이력구분 이력상세 등재구분
      2022 평가예정 계속평가 신청대상 (등재유지)
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      2002-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
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      2016 0.13 0.13 0.15
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