Comparison of physical–chemical properties of type I collagen from different species

Lin, Yung Kai; Liu, Deng Cheng

doi:10.1016/j.foodchem.2005.06.053

Cited by 163 publications

(135 citation statements)

References 24 publications

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“…The sample collagen was rich in glutamic acid, glycine, alanine, proline and hydroxyproline, with glycine representing nearly one-fourth of the total amino acid. According to previous studies, glycine was the most abundant amino acid in all collagens [12,20,30].…”

Section: Amino Acid Composition Of Turtle Lung Collagenmentioning

confidence: 87%

“…This property is used to express the integrity of the non-helical telopeptides when collagen is extracted and purified. The spectra were closely related to their higher proteinous contaminants which were not removed by the extraction procedures [30]. Figure 10 depicts the UV scanning spectrum of lung collagen obtained by the optimized enzymatic extraction method.…”

Section: Figure 8 Effect Of Hydrolysis Time On the Collagen Extractimentioning

confidence: 99%

“…The amino acid composition directly influenced the collagen's physical-chemical properties, like cross-linking ability and thermal stability [30]. Literatures indicated that the molecular structure of species is different and therefore results in a different structure of collagen.…”

Section: Amino Acid Composition Of Turtle Lung Collagenmentioning

confidence: 99%

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Extraction Optimization and Characterization of Collagen from the Lung of Soft-Shelled Turtle Pelodiscus Sinensis

Song¹,

Chen²,

Yang³

et al. 2014

IJNFS

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Abstract:The soft-shelled turtle (Pelodiscus sinensis) is a commercially important aquatic species with abundant collagen content and precious nutritious high quality goods. The present study was to optimize the collagen extraction from lung of Pelodiscus sinensis. Single-factor test was employed to investigate the effects of different extraction methods and the major factors that influence the collagen production in enzymatic extraction method on the collagen yield of lung. Optimization of the papain enzymatic extraction parameters was then examined using an orthogonal test design L9 (3 4 ). The optimum extraction conditions were obtained when the extraction temperature, papain enzyme dose, the ratio of solid to solution, and extraction time were 32°C, 4.0mg/ml, 1:35, and 12h, respectively. Under the optimized conditions, the collagen yield was up to 79.29%. The properties of turtle lung collagen were characterized by SDS-PAGE, UV scanning, and amino acid analysis. The results showed that the extracted lung collagen had high imino acid content at 21.8% and contained two α chains, β, and γ-components, belonging to the typical type I collagen. The amphibious aquatic turtle collagen is thought to be a viable novel source for replacement of terrestrial mammals and could provide scientific reference for the development of collagen polypeptide for terrapin animals.

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Section: Amino Acid Composition Of Turtle Lung Collagenmentioning

confidence: 87%

Section: Figure 8 Effect Of Hydrolysis Time On the Collagen Extractimentioning

confidence: 99%

See 1 more Smart Citation

Extraction Optimization and Characterization of Collagen from the Lung of Soft-Shelled Turtle Pelodiscus Sinensis

Song¹,

Chen²,

Yang³

et al. 2014

IJNFS

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“…Moreover, the biodegradation rates were accelerated with the materials having higher PS collagen ratio. Basic biochemical properties of different collagen origin were precisely measured in the previous study [10] and revealed that the PS collagen bounded with a relatively large amount of glycosaminoglycan and resulted in high enzymes resistance. The resistance to collagenase of HACSMs should be enhanced by PS collagen due to its relatively large amount of glycosaminoglycan, sterically hindering access to collagenase active sites.…”

Section: Discussionmentioning

confidence: 99%

Studies of Novel Hyaluronic Acid-collagen Sponge Materials Composed of Two Different Species of Type I Collagen

Lin

Liu

2006

J Biomater Appl

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ABSTRACT:The authors have developed novel hyaluronic acid (HA)-collagen sponge materials (HACSMs) composed of various ratios of bird feet (BF) and pig skin (PS) collagen that are fabricated employing a combination of freezing, lyophilizing, and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) crosslinking methods. Morphology, swelling ratio, resistance to collagenase, thermal stability, tensile strength, and free amine index are determined to evaluate the physical-chemical properties of various HACSMs. Different BF: PS ratios directly vary with the physical-chemical properties of HACSMs and control their biodegradability for multiple uses. Resistance to collagenase, thermal stability, and tensile strength of HACSMs increases as the ratio of BF collagen increases. On the contrary, the higher swelling ratio, free amine index, and pore size occur in materials composed of higher ratios of PS collagen. A linear relationship between the decreased ratio of PS collagen and the increase in tensile strength and biostability are observed. The materials of B4P1HA (BF : PS : HA ¼ 4 : 1 : 0.2) exhibit the highest value of tensile strength, but no significant difference exists between B4P1HA and B5P0HA (BF : PS : HA ¼ 5 : 0 : 0.2). These phenomena should be closely related to the BF collagen which contains a higher amount of carboxyl groups of glutamic or aspartic acid residues and forms more amine bonds under EDC cross-linking *Author to whom correspondence should be addressed. E-mail: nitrite.tw@gmail.com when compared to PS collagen. However, these results suggest that the B4P1HA and B5P0HA materials should be produced according to highest bio-stability and mechanical strength and, furthermore they may be suitable for artificial skin or drug delivery applications. JOURNAL OF BIOMATERIALS APPLICATIONS

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“…One of the prospective sources comes from marine organisms (sea urchins, fish scale and skin, jellyfish, shark skin). Many studies indicated that bird feet, frog skin, sea urchin and shark skin collagen have a molecular structure different than domestic animals [10][11][12]. Their amino acid composition, peptide constitution, glycosaminoglycan content and thermal behavior are significantly different from land animals.…”

mentioning

confidence: 99%

An Estimation of the Biological Properties of Fish Collagen in an Experimental In Vitro Study

Kuzan¹,

Smulczyńska-Demel²,

Chwiłkowska³

et al. 2015

Adv Clin Exp Med

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Background. The principal sources of medical collagen are pork, calf skin and bone. There are now more studies on a much safer, alternative source of active collagen, mainly from aquatic life. Active collagen and its peptides FCP (fish collagen peptides) have already been extracted from the skin of salmon, cobia, hoki, tilapia, zebrafish, ling, shark, silver carp and also jellyfish. Objectives. The aim of the study is to evaluate the effect of fish collagen on human fibroblasts from gingiva. The cytotoxicity of the new formulation and induction of endogenous collagen was estimated by means of the collagen derived from fish skin. Material and Methods. Fish collagen was extracted from the skin of silver carp at 16 degrees Celsius. To compare the biocompatibility and endogenous collagen production Geistlich Bio-Gide ® membrane was ordered in Geistlich Biomaterials (Geistich AG, Wolhusen, Switzerland). The culture of human fibroblasts was performed acc. to Saczko et al. The fibroblasts were treated 96 hours with 1.0%, 0.5% and 0.1% experimental collagen formulation to induce endogenous collagen production. The Sircol collagen assay was done to measure amount of collagen. Cell viability was assessed by measuring mitochondrial activity in MTT assay after 24 h followed by 24 h of incubation with experimental collagen formulation. Qualitative analysis was performed by immunocytochemically staining of collagen type I and III. Results. Preparations of fish collagen are not cytotoxic at concentrations below 1%. Cells cultured in the presence of this product are characterized by a large number of endogenous collagen, which is comparable to the control. In case of porcine collagen membrane was noticed decreased to 83% production of endogenous collagen and reduction of cell viability to 69%. Conclusions. Our study showed that experimental fish collagen is an innovative product which may induce expression of endogenous collagen in fibroblasts (Adv Clin Exp Med 2015, 24, 3, 385-392).

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Comparison of physical–chemical properties of type I collagen from different species

Cited by 163 publications

References 24 publications

Extraction Optimization and Characterization of Collagen from the Lung of Soft-Shelled Turtle Pelodiscus Sinensis

Extraction Optimization and Characterization of Collagen from the Lung of Soft-Shelled Turtle Pelodiscus Sinensis

Studies of Novel Hyaluronic Acid-collagen Sponge Materials Composed of Two Different Species of Type I Collagen

An Estimation of the Biological Properties of Fish Collagen in an Experimental In Vitro Study

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