Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros)

Ahmad, Mehraj; Benjakul, Soottawat; Nalinanon, Sitthipong

doi:10.1016/j.foodhyd.2010.03.001

Cited by 85 publications

(78 citation statements)

References 30 publications

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“…As shown in Table 1, glycine contents of ASC-G and PSC-G (359.3-362.5 residues/1000 residues) was higher than that of ASC-P and PSC-P (342.8-349.8 residues/1000 residues), and those reported for giant grouper, unicorn leatherjacket and bester sturgeon (319-344 residues/1000 residues) (Ahmad et al, 2010;Zhang et al, 2014b;Hsieh et al, 2016). The imino acid contents of collagens derived from the skin byproducts of paddlefish and globefish were 194.1-197.9 and 186.4-189.7 residues/1000 residues, respectively, which were analogous to that of unicorn leatherjacket (187-190 residues/1000 residues) (Ahmad et al, 2010), whilst higher than those of cold water fish such as cod and deep-sea redfish (154 and 165 residues/1000 residues) (Wang et al, 2008;Zhang et al, 2009a).…”

Section: Amino Acid Compositionmentioning

confidence: 75%

“…The imino acid contents of collagens derived from the skin byproducts of paddlefish and globefish were 194.1-197.9 and 186.4-189.7 residues/1000 residues, respectively, which were analogous to that of unicorn leatherjacket (187-190 residues/1000 residues) (Ahmad et al, 2010), whilst higher than those of cold water fish such as cod and deep-sea redfish (154 and 165 residues/1000 residues) (Wang et al, 2008;Zhang et al, 2009a). The less content of imino acid could lead to inferior thermal stability and lower melting point (Singh et al, 2011).…”

Section: Amino Acid Compositionmentioning

confidence: 94%

“…We believe both paddlefish and globefish skin byproducts can be the potential sources for collagen production, the market value of fish offal would be increased and the environmental pollution could be reduced. Currently, collagen from skin byproducts have been extracted from Spanish mackerel, unicorn leatherjacket, giant grouper and Nile perch (Muyonga et al, 2004;Ahmad et al, 2010;Hsieh et al, 2016). Nevertheless, there is scarce information that systematically investigates collagen from paddlefish and globefish.…”

Section: Introductionmentioning

confidence: 99%

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Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

2017

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Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin byproducts of paddlefish (ASC-P and PSC-P) and globefish (ASC-G and PSC-G) were purified and characterized. The imino acid contents of ASC-P, PSC-P, 197.9, 186.4 and 189.7 residues/1000 residues, respectively. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) confirmed that all four samples composed of two different α1-and α2-chains with integrated triple-helical structure. Denaturation temperatures of ASC-P, PSC-P, ASC-G and PSC-G were 29.6, 28.2, 27.4 and 26.9 °C, respectively. Based on Transmission electron microscopy (TEM) observation, all four samples could assemble into fibrils in vitro with D-periodicity. However, the fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Scanning electron microscopy (SEM) analysis confirmed well-defined fibril morphologies,the diameter of fibrils from ASC-P and PSC-P was thicker than those of ASC-G and PSC-G after 24 h incubation. These results indicated that paddlefish and globefish skin collagens could be alternatives to terrestrial collagens for applications in food-packaging, nutraceutical and pharmaceutical industries.Keywords: paddlefish; globefish; collagen; physicochemical property; fibril-forming property; fibril morphology.Practical Application: Utilization of paddlefish and globefish skin byproducts by extracting collagen with good physicochemical and fibril-forming properties.

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Section: Amino Acid Compositionmentioning

confidence: 75%

Section: Amino Acid Compositionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

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Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

2017

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“…The bone section specimens that were used in our study had been dried and fixed in CaF 2 plates, because of which, the observations did not show any HOH bending mode. A signal (amide I) with a characteristic strong absorbance on the spectrum originates mainly from the CO stretching mode involved in the binding of peptides responsible for forming the protein backbone [24][25][26] . This signal has often been used as a marker in the secondary structure analysis of proteins in liquid solutions.…”

Section: Discussionmentioning

confidence: 99%

“…The amide II band originates from the NH-bending mode accompanying the CN stretching mode, and the shift toward a lower wavenumber indicates the presence of hydrogen bonds 27,28) . The amide III band shows an infrared absorption attributable to the vibrations of CH 2 groups from a glycine backbone and a proline side chain, as well as to the peak combining the infrared absorption of the CN stretching mode and that of the NH bending mode from the amide bond 24) . Thus, identification of amide bands in the infrared spectrum indicated the presence of remaining protein in the decalcifi ed samples.…”

Section: Discussionmentioning

confidence: 99%

Analysis of Demineralized Mammalian Bone Tissue by Fourier Transform Infrared Microscopy

Yamaguchi

Yamamoto

Tsujigiwa

2018

J. Hard Tissue Biology.

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The amounts and properties of cartilage matrix components such as collagen and proteoglycans change in joint and bone related diseases, and spectroscopic studies of these components are important for developing new diagnostic and therapeutic methods. Infrared spectroscopy provides information on chromophores and vibrations related to characteristic molecules present in cells and tissues. In addition, infrared spectroscopy is a non-invasive and useful spectroscopy based analytical technique that does not use antibody labeling. In this study, we used decalcifi ed unstained specimens of canine mandibular bone and rat and rabbit tibia. The specimens were subjected to microscopic infrared spectroscopy, and analyzed by determining the infrared spectrum, with a focus on fi ber proteins (collagen) and carbohydrates (proteoglycans) present in the specimens. Normally, a large signal originating from the PO stretching mode of phosphate (PO 4 3-) is observed during measurements of the infrared absorption spectrum of bone sections; however, the above mentioned signal was not observed in our study as the samples used in our study were decalcifi ed. Instead, we observed signals from proteoglycans that are usually masked by signals originating from PO stretching and are diffi cult to observe. Measurements were performed on the same types of bone sections, and the results showed that the infrared spectrum varied greatly depending on the portion subjected to the measurements. However, in contrast, the results of the measurements conducted on the cartilage regions of rat and rabbit tibia coincided in terms of the amide I, amide II, and amide III bands, as well as the signal intensity ratio of the proteoglycan signal. Our fi ndings indicated that infrared spectrum patterns allowed the identifi cation of cartilaginous tissues in bone sections. By using this characteristic signal as a marker and carrying out two dimensional mapping on the cartilage part, for example, it is suggested that it can be applied to analysis of collagen distribution in demineralized fossil samples.

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Processing and Industrial Aspects of Fish‐scale Collagen: A Biomaterials Perspective

Dhara

Datta

Pal

et al. 2013

Marine Proteins and Peptides

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Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros)

Cited by 85 publications

References 30 publications

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

Analysis of Demineralized Mammalian Bone Tissue by Fourier Transform Infrared Microscopy

Processing and Industrial Aspects of Fish‐scale Collagen: A Biomaterials Perspective

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