scholarly journals Extraction and Properties of Acid-Soluble Collagen and Pepsin-Soluble Collagen from Silver Carp (Hypophthalmichthys molitrix) Scales: Prerequisite Information for Fishery Processing Waste Reuse

2019 ◽  
Vol 28 (4) ◽  
pp. 2923-2930 ◽  
Author(s):  
Jiacheng Wu ◽  
Lili Kong ◽  
Jinwei Zhang ◽  
Wuyong Chen
Keyword(s):  
Silver Carp ◽  
Hypophthalmichthys Molitrix ◽  
Processing Waste ◽  
Waste Reuse ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Pepsin Soluble Collagen

Characterisation of acid-soluble collagen from skin of silver carp (Hypophthalmichthys molitrix)

2009 ◽  
Vol 116 (1) ◽  
pp. 318-322 ◽  
Author(s):  
Junjie Zhang ◽  
Rui Duan ◽  
Yuanyong Tian ◽  
Kunihiko Konno
Keyword(s):  
Silver Carp ◽  
Hypophthalmichthys Molitrix ◽  
Soluble Collagen ◽  
Acid Soluble Collagen

Extraction and Partial Characterization of Pepsin-Soluble Collagens from the Skin of Amiurus Nebulosus

2011 ◽  
Vol 236-238 ◽  
pp. 2926-2934 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Hua Liu ◽  
Run Feng Wu
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
Skin Collagen ◽  
Maximal Yield ◽  
Pepsin Soluble Collagen

Pepsin-soluble collagen (PSC) was successfully extracted from the skin of Amiurus nebulosus. The skin of Amiurus nebulosus was immersed in 0.3 mol/L acetic acid (1: 20, m: V) for 6 h at 37°C, while pepsin was added, at a level of 5000U/g dosage of defatted skin. The maximal yield of the collagen was 97.44%, which was higher than that of acid-soluble collagen (ASC) at 62.05%. Some properties of pepsin-soluble collagens from the skin of Amiurus nebulosus were characterized. Amino acid composition and SDS-PAGE suggested that the collagen might be classified as type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements in PSC of Amiurus nebulosus skin of collagen. There is a possibility to use Amiurus nebulosus skin collagen as an alternative source of collagen for industrial purposes and subsequently it may maximize the economical value of the fish.

scholarly journals Characterization of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) extracted from shortfin scad (Decapterus macrosoma) waste

Food Research ◽  
2020 ◽  
Vol 4 (6) ◽  
pp. 2272-2280
Author(s):  
A.W. Sulaiman ◽  
N.M. Sarbon
Keyword(s):  
Chemical Composition ◽  
Protein Concentration ◽  
Food Ingredient ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Kjeldahl Method ◽  
Biuret Method ◽  
The Rich ◽  
Pepsin Soluble Collagen

Fish waste management is one of the biggest impacts towards the environment. However, it is one of the rich sources of protein. Therefore, the aim of this study was to isolate and characterize acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from shortfin scad (Decapterus macrosoma) waste, with the yields of ASC (3.35±3.43%) and PSC (0.10±0.13%) respectively. The isolated ASC and PSC from shortfin scad waste were characterized on chemical composition, protein concentration, structural properties by FTIR, solubility and morphology properties compared to the commercial collagen from tilapia (Oreochromis niloticus) scales. In terms of chemical composition, PSC showed better than ASC, since it contains comparatively higher in protein (26.97±1.02%) by Kjeldahl method and protein concentration (2.69±0.47 mg/mL) by biuret method, compared to ASC. The FTIR investigations also certified the existence of spacial triplehelical structures of collagens that are important for collagen backbones. Solubility results showed that both ASC and PSC are high insolubility at acidic pH with the lowest solubilisation point at the range of alkali condition. The morphological analysis of both ASC and PSC were almost similar too, as there were fibrils and porous structure. Therefore, collagen from shortfin scad waste, could be a useful alternative, with the potential to be used in food ingredient, biomedical, pharmaceutical and nutraceuticals industries

scholarly journals Extraction and characterization of acid-soluble collagen and pepsin-soluble collagen from the dry scales of the striped snakehead (Channa striatus)

2018 ◽  
Vol 21 (3) ◽  
pp. 513
Author(s):  
Bagus Fajar Pamungkas ◽  
Supriyadi Supriyadi ◽  
Agnes Murdiati ◽  
Retno Indrati
Keyword(s):  
Type I Collagen ◽  
Raw Materials ◽  
Acid Group ◽  
Extraction Methods ◽  
Type I ◽  
Channa Striatus ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Imino Acid ◽  
Pepsin Soluble Collagen

Characteristics of collagen are influenced by the source of raw materials and extraction methods used. The aim of this research was to characterize the acid- and pepsin-soluble collagens from the dry scales of the striped snakehead (Channa striatus). Collagen was extracted using to methods including 0.5 M acetic acid and 0.1% pepsin. The yield of acid soluble collagen (KLA-SH) and pepsin soluble collagen (KLP-SH) were 0.98% and 1.94%, respectively. KLA-SH and KLP-SH contained glycine as the major amino acid and had high imino acid group content i.e 226 and 230 residues/1.000 residues, respectively. FTIR spectra of KLA-SH and KLP-SH showed that of the structure of collagen could be maintained in the form of triple helix structure. KLA-SH and KLP-SH consisted of α1- and α2-chain, β-chain, and γ-chain and is suggested as type I collagen.

scholarly journals Isolation and characterization of acid and pepsin soluble collagen extracted from sharpnose stingray (Dasyatis zugei) skin

Food Research ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
T.Y. Ong ◽  
M.I. Shaik ◽  
N.M. Sarbon
Keyword(s):  
Helical Structure ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Isolation And Characterization ◽  
Fibrous Network ◽  
Acid Soluble Collagen ◽  
Maximum Temperatures ◽  
Surface Morphologies ◽  
Pepsin Soluble Collagen

This study aimed to isolate and characterize the acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of the sharpnose stingray (Dasyatis zugei). Isolated ASC and PSC were subjected to chemical and physical characterizations. The yield of PSC (34.84±1.26%) was significantly higher than that of ASC (20.48±4.41%) (p<0.05). There were no significant differences between ASC and PSC in terms of chemical composition (p>0.05). Both ASC and PSC were thermally stable at high temperatures, with denaturation temperatures of 24.1°C and 25.2°C, respectively, and maximum temperatures of 31.94±0.13°C and 31.79±0.23°C, respectively. Fourier transform infrared (FTIR) investigations showed the presence of triple helical structure with strong hydrogen bonding in both ASC and PSC. Meanwhile, both collagens were highly solubilized at acidic pH but at different optimal pH. The surface morphologies of ASC and PSC were loose and possessed slender, less uniform and irregular fibrous network structures with large and irregular pores observed between the fibrils. This finding showed that the alternative source of marine collagen possesses good physicochemical properties which highly potential for nutraceutical, pharmaceutical or cosmeceutical application.

Isolation and characterisation of acid- and pepsin-soluble collagen from the skin of Cervus korean TEMMINCK var. mantchuricus Swinhoe

2018 ◽  
Vol 58 (3) ◽  
pp. 585 ◽  
Author(s):  
Gaurav Lodhi ◽  
Yon-Suk Kim ◽  
Eun-Kyung Kim ◽  
Jin-Woo Hwang ◽  
Hyung-Sik Won ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Thermal Denaturation ◽  
Peptide Hydrolysis ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Thermal Denaturation Temperature ◽  
Skin Collagen ◽  
Pepsin Soluble Collagen ◽  
Calf Skin

Acid-soluble collagen and pepsin-soluble collagen were extracted from the skin of deer, Cervus korean TEMMINCK var. mantchuricus Swinhoe. The two types of collagen were then characterised using sodium dodecyl sulfate–polyacrylamide gel electrophoresis, amino acid composition analysis, peptide hydrolysis patterns, thermal denaturation temperature, differential scanning calorimetry, Fourier transform infrared spectroscopy, and nuclear magnetic resonance imaging. The yield of pepsin-soluble collagen (9.62%) was greater than that of acid-soluble collagen (2.24%), but both types of collagen showed similar electrophoretic patterns with each other and with calf skin collagen. The peptide hydrolysis pattern results suggested that calf skin collagen and pepsin-soluble collagen from deer skin may be similar in terms of their primary structure. The thermal denaturation temperature of acid-soluble collagen and pepsin-soluble collagen were 36.67°C and 36.44°C, respectively, and their melting temperatures were 110°C and 120°C, respectively, which suggest high thermal stability. Fourier transform infrared showed a triple helical structure and nuclear magnetic resonance confirmed the presence of ‘hydration’ water. These results provide a basis for large-scale production and further application as alternatives to other mammalian collagens.

Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus)

2011 ◽  
Vol 129 (3) ◽  
pp. 1179-1186 ◽  
Author(s):  
Kanokwan Matmaroh ◽  
Soottawat Benjakul ◽  
Thummanoon Prodpran ◽  
Angel B. Encarnacion ◽  
Hideki Kishimura
Keyword(s):  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Pepsin Soluble Collagen

Effect of Different Factors on the Viscosity of Collagen from Amiurus nebulosus Skin

2013 ◽  
Vol 781-784 ◽  
pp. 1723-1727 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Mei Lan Yuan ◽  
Wei Su ◽  
Hua Liu
Keyword(s):  
Storage Time ◽  
Ph Value ◽  
Effect Of Ph ◽  
Standing Time ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Pepsin Soluble Collagen

The different factors of influencing viscosity of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from Amiurus nebulosus skin were studied. Influence of concentration, pH value, temperature and standing time on their viscosity properties were tested. The results showed that the viscosity of ASC and PSC increase with the increasing of the concentration of collagens, and decreased with the increasing of temperature. And the viscosity decreased at first with the prolonging of the storage time, after that increased up to maximum, then decreased again. The effect of pH on viscosity is very complex, the maximum viscosity value of ASC and PSC were at pH 7.0.

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