Tissues rely on collagen for structural and biological integrity,as well as for function and strength.Several collagen sources have been investigated due to its wide variety of applications,such as collagen from cows ...Tissues rely on collagen for structural and biological integrity,as well as for function and strength.Several collagen sources have been investigated due to its wide variety of applications,such as collagen from cows and pigs.However,mammalian-based collagen has been limited by diseases like bovine spongiform encephalopathy(BSE)and other religious limitations.Hence,fish collagen has caught the attention of the research community because it is easy to extract,has a high level of collagen content,excellent absorption properties,a low molecular weight,biocompatibility,little risk of disease transmission from animals to humans,negligible environmental contamination,and fewer ethical and religious concerns,posing as an ideal resource for product development.This review focuses on the growing role of marine collagen in the advances of various biomedical applications,such as drug delivery,tissue engineering,regeneration,and wound healing,which will be covered in depth.展开更多
To study the current application and development of fish scale collagen at home and abroad, this paper reviews the structural properties, methods of extracting collagen from fish scale and the applications of collagen...To study the current application and development of fish scale collagen at home and abroad, this paper reviews the structural properties, methods of extracting collagen from fish scale and the applications of collagen in biological medicine, food and chemical industries, cosmetics and other fields, discusses the utilization value of fish scale collagen, to provide a theoretical basis for future development and application of fish scale collagen.展开更多
A novel enzymatic method for extraction and preparation of fish collagen from swim bladder revealed the occurrence of α, β and γ bands with approximately 12.1 g/100g collagen corresponding to 89% of collagen and th...A novel enzymatic method for extraction and preparation of fish collagen from swim bladder revealed the occurrence of α, β and γ bands with approximately 12.1 g/100g collagen corresponding to 89% of collagen and thus confirmed the nativity and purity of the fish collagen. FT-IR studies confirmed the retention of all three amide bands of I, II and III, and triple helixcity. UN-crosslinked and UV-crosslinked fish collagen membrane records a very high temperature of helix denaturation at 197℃ and 215℃, shrinkage temperature at 50℃ ± 3.2℃ and 62℃ ± 2.7℃ and tensile strength at 16.89 ± 2.5 and 120.02 ± 1.0 Kg/cm2 respectively. Fish collagen matrix promoted NIH 3T3 and L6 cellular growth and proliferation. The study indicates that availability of pure fish collagen could replace bovine collagen in tissue engineering applications.展开更多
Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two differen...Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.展开更多
To make more effective use of underutilized resources, pepsin-solubilized collagen (PSC) was successfully extracted from the skin of black carp (Mylopharyngdon piceus) with a yield of 45.7% based on dry weight. The PS...To make more effective use of underutilized resources, pepsin-solubilized collagen (PSC) was successfully extracted from the skin of black carp (Mylopharyngdon piceus) with a yield of 45.7% based on dry weight. The PSC comprising two identical α1-chains and one α2-chain with no disulfide bond was characterized as type I, and it contained 195 imino acid residues vs. 1000 amino acid residues. The collagen showed an absorption edge around 218 nm, which was lower than the maximum absorption wavelength of other PSC. The denaturation temperature of PSC was 25.6°C, which was lower than that of porcine collagen by approximately 11°C. The isoelectric point (pI) was estimated to be 8.23, and the collagen was soluble at an acidic pH as well as below 40 g/L NaCl. It is thought that the high yield and stability of PSC from the skin of black carp warrant its application as a new source of collagen for industrial purposes.展开更多
基金supported by grants from the National Key Research and Development Program of China(2020YFA0908200).
文摘Tissues rely on collagen for structural and biological integrity,as well as for function and strength.Several collagen sources have been investigated due to its wide variety of applications,such as collagen from cows and pigs.However,mammalian-based collagen has been limited by diseases like bovine spongiform encephalopathy(BSE)and other religious limitations.Hence,fish collagen has caught the attention of the research community because it is easy to extract,has a high level of collagen content,excellent absorption properties,a low molecular weight,biocompatibility,little risk of disease transmission from animals to humans,negligible environmental contamination,and fewer ethical and religious concerns,posing as an ideal resource for product development.This review focuses on the growing role of marine collagen in the advances of various biomedical applications,such as drug delivery,tissue engineering,regeneration,and wound healing,which will be covered in depth.
基金Supported by Scientific Research Project of Ezhou Polytechnic(2016YBA51)Science and Technology Research Project of Hubei Provincial Department of Education(B2017531)
文摘To study the current application and development of fish scale collagen at home and abroad, this paper reviews the structural properties, methods of extracting collagen from fish scale and the applications of collagen in biological medicine, food and chemical industries, cosmetics and other fields, discusses the utilization value of fish scale collagen, to provide a theoretical basis for future development and application of fish scale collagen.
文摘A novel enzymatic method for extraction and preparation of fish collagen from swim bladder revealed the occurrence of α, β and γ bands with approximately 12.1 g/100g collagen corresponding to 89% of collagen and thus confirmed the nativity and purity of the fish collagen. FT-IR studies confirmed the retention of all three amide bands of I, II and III, and triple helixcity. UN-crosslinked and UV-crosslinked fish collagen membrane records a very high temperature of helix denaturation at 197℃ and 215℃, shrinkage temperature at 50℃ ± 3.2℃ and 62℃ ± 2.7℃ and tensile strength at 16.89 ± 2.5 and 120.02 ± 1.0 Kg/cm2 respectively. Fish collagen matrix promoted NIH 3T3 and L6 cellular growth and proliferation. The study indicates that availability of pure fish collagen could replace bovine collagen in tissue engineering applications.
文摘Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.
文摘To make more effective use of underutilized resources, pepsin-solubilized collagen (PSC) was successfully extracted from the skin of black carp (Mylopharyngdon piceus) with a yield of 45.7% based on dry weight. The PSC comprising two identical α1-chains and one α2-chain with no disulfide bond was characterized as type I, and it contained 195 imino acid residues vs. 1000 amino acid residues. The collagen showed an absorption edge around 218 nm, which was lower than the maximum absorption wavelength of other PSC. The denaturation temperature of PSC was 25.6°C, which was lower than that of porcine collagen by approximately 11°C. The isoelectric point (pI) was estimated to be 8.23, and the collagen was soluble at an acidic pH as well as below 40 g/L NaCl. It is thought that the high yield and stability of PSC from the skin of black carp warrant its application as a new source of collagen for industrial purposes.
