The interactions of collagen and sericin were studied by fluorescence spectra, ultraviolet spectra, FTIR spectra and dynamic light scattering. The fluorescence quenching in emission spectra and red-shift (283-330nm) in synchronous fluorescence spectra suggested the Tyr of collagen and sericin overlapped with a distance of 3Å, generating excimer. The overlapped Tyr of collagen and sericin decreased the hydrophobicity of collagen, which resulted in the red-shifts (233-240nm) in ultraviolet spectra. Moreover, the red-shifts of amide bands of collagen in FTIR spectra indicated the hydrogen bonds of collagen were weaken and it could also be explained by the overlapped Tyr. The results of 2D-FTIR spectra demonstrated the backbone of collagen molecule was varied and the most susceptible structure of collagen was the triple helix with the presence of sericin. Based on dynamic light scattering, we conjectured large pure collagen aggregates were replaced by hybrid aggregates of collagen and sericin particles after the addition of sericin. With ascending sericin ratio, the diameters of the hybrid aggregates increased and attained maximum with 60% ratio of sericin, which were on account of the increasing excimer number. The results of DSC demonstrated the presence of sericin enhanced the thermal stability of collagen.
Keywords: Blending; Collagen; Sericin.
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