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To improve the mechanical properties and confer antimicrobial activity, transglutaminase (TGase) was used as a cross-linking agent and lysozyme (LYS) was incorporated as an antimicrobial agent to prepare novel active tilapia collagen (TC) films. While the difference in visual appearance was not obvious, the LYS incorporation increased the opacity of TC films. The water vapor permeability of all TGase cross-linked TC films was significantly (p < 0.05) lower than that of the control film (prepared without TGase and LYS). In addition, while the tensile strength and Young's modulus of all TGase cross-linked TC films were significantly (p < 0.05) higher than those of the control film, elongation at break of all TGase cross-linked TC films was significantly (p < 0.05) lower than that of the control film. LYS incorporated TC films showed antimicrobial activity against E. coli, Staphylococcus aureus, Enterococcus faecium, Bacillus subtilis and Pseudomonas fluorescens. Collectively, TC films with improved physiochemical properties and antimicrobial activity have a good potential to serve as active food packaging materials. [ABSTRACT FROM AUTHOR]

To improve the mechanical properties and confer antimicrobial activity, transglutaminase (TGase) was used as a cross-linking agent and lysozyme (LYS) was incorporated as an antimicrobial agent to prepare novel active tilapia collagen (TC) films. While the difference in visual appearance was not obvious, the LYS incorporation increased the opacity of TC films. The water vapor permeability of all TGase cross-linked TC films was significantly (p < 0.05) lower than that of the control film (prepared without TGase and LYS). In addition, while the tensile strength and Young’s modulus of all TGase cross-linked TC films were significantly (p < 0.05) higher than those of the control film, elongation at break of all TGase cross-linked TC films was significantly (p < 0.05) lower than that of the control film. LYS incorporated TC films showed antimicrobial activity against E. coli, Staphylococcus aureus, Enterococcus faecium, Bacillus subtilis and Pseudomonas fluorescens. Collectively, TC films with improved physiochemical properties and antimicrobial activity have a good potential to serve as active food packaging materials.

Abstract Background Collagen is the most abundant structural protein in the mammalian connective tissue and represents approximately 30% of animal protein. The current study evaluated the potential capacity of collagen extract derived from Nile tilapia skin in improving the cutaneous wound healing in rats and investigated the underlying possible mechanisms. A rat model was used, and the experimental design included a control group (CG) and the tilapia collagen treated group (TCG). Full-thickness wounds were conducted on the back of all the rats under general anesthesia, then the tilapia collagen extract was applied topically on the wound area of TCG. Wound areas of the two experimental groups were measured on days 0, 3, 6, 9, 12, and 15 post-wounding. The stages of the wound granulation tissues were detected by histopathologic examination and the expression of vascular endothelial growth factor (VEGF), and transforming growth factor (TGF-ß1) were investigated using immunohistochemistry. Moreover, relative gene expression analysis of transforming growth factor-beta (TGF-ß1), basic fibroblast growth factor (bFGF), and alpha-smooth muscle actin (α-SMA) were quantified by real-time qPCR. Results The histopathological assessment showed noticeable signs of skin healing in TCG compared to CG. Immunohistochemistry results revealed remarkable enhancement in the expression levels of VEGF and TGF-β1 in TCG. Furthermore, TCG exhibited marked upregulation in the VEGF, bFGF, and α-SMA genes expression. These findings suggested that the topical application of Nile tilapia collagen extract can promote the cutaneous wound healing process in rats, which could be attributed to its stimulating effect on recruiting and activating macrophages to produce chemotactic growth factors, fibroblast proliferation, and angiogenesis. Conclusions The collagen extract could, therefore, be a potential biomaterial for cutaneous wound healing therapeutics.

Water bodies purvey plenty of natural resources that are utilized to manufacture materials or are employed as novel medicines in medical and dental practice. Among sponges, corals, fishes, and other marine life forms, one promising source is the “tilapia fish.” It is principally farmed for the utilization and construction of therapeutic biomaterials. As oral physicians or dental practitioners, we grapple with many oral lesions and wounds in routine practice, “burns” being one of them. Tilapia skin and its collagen are being applied for dermatological burns. Since the branch of medicine encourages innovative ideas and research work in the treatment of challenging oral lesions, this article aims to communicate the idea of its usefulness in oral burns and alike lesions, making tilapia a neoteric healing agent, keeping in mind the remarkable biological properties it possesses.

Fish collagen has recently been reported to be a novel biomaterial for cell and tissue culture as an alternative to conventional mammalian collagens such as bovine and porcine collagens. Fish collagen could overcome the risk of zoonosis, such as from bovine spongiform encephalopathy. Among fish collagens, tilapia collagen, the denaturing temperature of which is near 37°C, is appropriate for cell and tissue culture. In this study, we investigated chondrogenic differentiation of human mesenchymal stem cells (hMSCs) cultured on tilapia scale collagen fibrils compared with porcine collagen and non-coated dishes. The collagen fibrils were observed using a scanning electronic microscope. Safranin O staining, glycosaminoglycans (GAG) expression, and real-time PCR were examined to evaluate chondrogenesis of hMSCs on each type of collagen fibril. The results showed that hMSCs cultured on tilapia scale collagen showed stronger Safranin O staining and higher GAG expression at day 6. Results of real-time PCR indicated that hMSCs cultured on tilapia collagen showed earlier SOX9 expression on day 4 and higher AGGRECAN and COLLAGEN II expression on day 6 compared with on porcine collagen and non-coated dishes. Furthermore, low mRNA levels of bone gamma-carboxyglutamate, a specific marker of osteogenesis, showed that tilapia collagen fibrils specifically enhanced chondrogenic differentiation of hMSCs in chondrogenic medium, as well as porcine collagen. Accordingly, tilapia scale collagen may provide an appropriate collagen source for hMSC chondrogenesis in vitro. [ABSTRACT FROM AUTHOR]

Fish collagen has recently been reported to be a novel biomaterial for cell and tissue culture as an alternative to conventional mammalian collagens such as bovine and porcine collagens. Fish collagen could overcome the risk of zoonosis, such as from bovine spongiform encephalopathy. Among fish collagens, tilapia collagen, the denaturing temperature of which is near 37°C, is appropriate for cell and tissue culture. In this study, we investigated chondrogenic differentiation of human mesenchymal stem cells (hMSCs) cultured on tilapia scale collagen fibrils compared with porcine collagen and non-coated dishes. The collagen fibrils were observed using a scanning electronic microscope. Safranin O staining, glycosaminoglycans (GAG) expression, and real-time PCR were examined to evaluate chondrogenesis of hMSCs on each type of collagen fibril. The results showed that hMSCs cultured on tilapia scale collagen showed stronger Safranin O staining and higher GAG expression at day 6. Results of real-time PCR indicated that hMSCs cultured on tilapia collagen showed earlier SOX9 expression on day 4 and higher AGGRECAN and COLLAGEN II expression on day 6 compared with on porcine collagen and non-coated dishes. Furthermore, low mRNA levels of bone gamma-carboxyglutamate, a specific marker of osteogenesis, showed that tilapia collagen fibrils specifically enhanced chondrogenic differentiation of hMSCs in chondrogenic medium, as well as porcine collagen. Accordingly, tilapia scale collagen may provide an appropriate collagen source for hMSC chondrogenesis in vitro., (Copyright © 2016 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.)