Improving properties of silk sericin membranes via enzymatic oxidation with laccase and TEMPO.
Biotechnol Appl Biochem
; 65(3): 372-380, 2018 May.
Article
em En
| MEDLINE
| ID: mdl-28881487
ABSTRACT
Silk sericin has excellent features of antioxidant ability and good cytocompatibility; however, high water solubility and poor mechanical properties have restricted its application in biomedical fields. In this study, aimed at improving the mechanical properties of a regenerated silk sericin, the primary hydroxy groups in silk sericin were enzymatically oxidized by using laccase and 2,2',6,6'-tetramethylpiperidine-N-oxyl (TEMPO), and the generated reactive groups then reacted further with the amino groups in the sericin chains. The efficacy of the enzymatic cross-linking was evaluated by means of determination of amino groups, SDS polyacrylamide gel electrophoresis, Fourier transform infrared (FTIR) spectroscopy, and size exclusion chromatography. The results indicated that either laccase/TEMPO incubation or laccase treatment alone incurred a noticeable increase in the molecular weight of the sericin. FTIR analysis revealed that there was small change in the structure of the silk sericin after laccase/TEMPO treatment, and the obtained air-dried sericin membrane exhibited remarkably improved mechanical properties relative to those of the uncross-linked sericin membrane. In addition, the biocompatibility of the sericin membrane was at an acceptable level according to the cell viability of NIH/3T3 cells. The present work provides a novel method for the preparation of sericin-based biomaterials.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Materiais Biocompatíveis
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Óxidos N-Cíclicos
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Lacase
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Sericinas
Limite:
Animals
Idioma:
En
Revista:
Biotechnol Appl Biochem
Assunto da revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Ano de publicação:
2018
Tipo de documento:
Article