Cross-linking of collagen with laccases and tyrosinases

Oxidation of acid soluble collagen (ASC), collagen suspension and BrCN-peptides (BrCN-P) with tyrosinases from B. obtusa (BoT1, BoT2) and A. bisporus (AbT) and laccases from T. versicolor (TvL) and T. hirsuta (ThL) resulted in UV/VIS peaks at 475 nm and 305 nm indicating formation of reactive o-quin...

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Published inMaterials Science & Engineering C Vol. 31; no. 5; pp. 1068 - 1077
Main Authors Jus, S., Stachel, I., Schloegl, W., Pretzler, M., Friess, W., Meyer, M., Birner-Gruenberger, R., Guebitz, G.M.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 20.07.2011
Subjects
Collagen
Collagens
Compressive strength
Crosslinking
Degradation
Enzymes
Laccase
Microorganisms
Tyrosinase
Crosslinking
Collagen
Tyrosinase
Laccase
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Abstract Oxidation of acid soluble collagen (ASC), collagen suspension and BrCN-peptides (BrCN-P) with tyrosinases from B. obtusa (BoT1, BoT2) and A. bisporus (AbT) and laccases from T. versicolor (TvL) and T. hirsuta (ThL) resulted in UV/VIS peaks at 475 nm and 305 nm indicating formation of reactive o-quinones and cross-linked components. Concomitant oxygen consumption was higher for the low molecular weight enzymes (TvL and BoT2) indicating limited accessibility. SDS-PAGE and SEC bands at higher MW demonstrated the formation of cross-linked material. LC-MS/MS analysis suggested the involvement of tyrosine residues in cross-linking without major changes of sequence similarities to untreated collagen. However, an increase of the SEC α-peak together with a decrease of β-peak and the 1235/1450 cm − 1 ratio (FTIR) indicated partial degradation. Crosslinking was enhanced by phenolic molecules such as catechine which lead to increased denaturation temperature and reduced degradation by microbial collagenase. The tensile strength was increased whereas resistance to compressive forces was not influenced. [Display omitted] ► Enzymatic cross-linking of collagen with oxidoreductases demonstrated. ► Oxidation of collagen by laccase and tyrosinase proven. ► Applications potential of enzymatic collagen cross-linking in medical applications shown.
AbstractList Oxidation of acid soluble collagen (ASC), collagen suspension and BrCN-peptides (BrCN-P) with tyrosinases from B. obtusa (BoT1, BoT2) and A. bisporus (AbT) and laccases from T. versicolor (TvL) and T. hirsuta (ThL) resulted in UV/VIS peaks at 475 nm and 305 nm indicating formation of reactive o-quinones and cross-linked components. Concomitant oxygen consumption was higher for the low molecular weight enzymes (TvL and BoT2) indicating limited accessibility. SDS-PAGE and SEC bands at higher MW demonstrated the formation of cross-linked material. LC-MS/MS analysis suggested the involvement of tyrosine residues in cross-linking without major changes of sequence similarities to untreated collagen. However, an increase of the SEC α-peak together with a decrease of β-peak and the 1235/1450 cm − 1 ratio (FTIR) indicated partial degradation. Crosslinking was enhanced by phenolic molecules such as catechine which lead to increased denaturation temperature and reduced degradation by microbial collagenase. The tensile strength was increased whereas resistance to compressive forces was not influenced. [Display omitted] ► Enzymatic cross-linking of collagen with oxidoreductases demonstrated. ► Oxidation of collagen by laccase and tyrosinase proven. ► Applications potential of enzymatic collagen cross-linking in medical applications shown.
Oxidation of acid soluble collagen (ASC), collagen suspension and BrCN-peptides (BrCN-P) with tyrosinases from B. obtusa (BoT1, BoT2) and A. bisporus (AbT) and laccases from T. versicolor (TvL) and T. hirsuta (ThL) resulted in UV/VIS peaks at 475nm and 305nm indicating formation of reactive o-quinones and cross-linked components. Concomitant oxygen consumption was higher for the low molecular weight enzymes (TvL and BoT2) indicating limited accessibility. SDS-PAGE and SEC bands at higher MW demonstrated the formation of cross-linked material. LC-MS/MS analysis suggested the involvement of tyrosine residues in cross-linking without major changes of sequence similarities to untreated collagen. However, an increase of the SEC alpha -peak together with a decrease of beta -peak and the 1235/1450cm-1 ratio (FTIR) indicated partial degradation. Crosslinking was enhanced by phenolic molecules such as catechine which lead to increased denaturation temperature and reduced degradation by microbial collagenase. The tensile strength was increased whereas resistance to compressive forces was not influenced.
Author Meyer, M.
Stachel, I.
Birner-Gruenberger, R.
Schloegl, W.
Friess, W.
Pretzler, M.
Jus, S.
Guebitz, G.M.
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  surname: Schloegl
  fullname: Schloegl, W.
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  surname: Pretzler
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  email: guebitz@tugraz.at
  organization: Austrian Centre of Industrial Biotechnology ACIB, Petersgasse 14, 8010 Graz, Austria
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Snippet Oxidation of acid soluble collagen (ASC), collagen suspension and BrCN-peptides (BrCN-P) with tyrosinases from B. obtusa (BoT1, BoT2) and A. bisporus (AbT) and...
Oxidation of acid soluble collagen (ASC), collagen suspension and BrCN-peptides (BrCN-P) with tyrosinases from B. obtusa (BoT1, BoT2) and A. bisporus (AbT) and...
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elsevier
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StartPage 1068
SubjectTerms Collagen
Collagens
Compressive strength
Crosslinking
Degradation
Enzymes
Laccase
Microorganisms
Tyrosinase
Title Cross-linking of collagen with laccases and tyrosinases
URI https://dx.doi.org/10.1016/j.msec.2011.03.007
https://search.proquest.com/docview/889396899
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