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

Wu, Jiacheng; Kong, Lili; Zhang, Jinwei; Chen, Wuyong

doi:10.15244/pjoes/93742

Cited by 18 publications

(13 citation statements)

References 28 publications

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“…These results were higher than what was found by Bhagwat & Dandge (2016) when extracting collagen by acidic method from the scales of common carp, which amounted to 9.79%. Wu et al (2019) found that the collagen yield of Hypophthalmichthys molitrix fish scales was 5.09. Matmaroh et al (2011) reported that the yield of collagen extracted by the enzymatic method from the scales of the golden-spotted goatfish Parupeneus heptacanthus was 1.20%.…”

Section: Yield and Protein Content Of The Collagenmentioning

confidence: 99%

Production of Hydrolyzed Collagen from Common Carp Cyprinus carpio L. Scales by Synergistic Enzyme Systems

Al-Abadi

AI-Temimi

2022

Basrah J. Agric. Sci.

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Fish skin, bones and scales are a good source of collagen, for the sake of exploitation these fish wastes of high commercial worth and convert them into food, therapeutic and pharmaceutical products. Therefore, the study included extracting collagen with acetic acid at a concentration 0.5 M and pepsin enzyme 0.1% from fish Cyprinus carpio scales and then producing hydrolyzed collagen protein. Chemical content of the scales was estimated from the percentage of moisture, protein, fat and ash, as it was found (55.36, 35.85, 2.47 and 5.99) %, respectively. The metallic elements represented by (Ca, P, Fe and Zn), they reached (153430, 1887.5, 71.455 and 48.045) µg.g-1. The collagen yield by the two methods mentioned above was 16.40% and 5.30%, respectively. Diagnosis of collagen extracted with acid using FT-IR technique and determination of the active groups in it, the presence of amides A, B, I, II and III was observed at frequencies 3413.39, 2924.52, 1653.66, 1548.56 and 1240 cm-1, respectively. Hydrolysed collagen was prepared using Collagenase enzyme followed by Pepsin enzyme, the highest degree of hydrolysis reached 43.56% after four hours. The electrophoresis of collagen extracted with acid and enzyme was carried out, as three bundles of collagen α1, α2 and β were obtained with weights (126, 100 and 180) KD, respectively.

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Section: Yield and Protein Content Of The Collagenmentioning

confidence: 99%

Production of Hydrolyzed Collagen from Common Carp Cyprinus carpio L. Scales by Synergistic Enzyme Systems

Al-Abadi

AI-Temimi

2022

Basrah J. Agric. Sci.

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“…Moreover, the distribution of molar mass, structure and composition, and the subsequent functional features and properties of collagen, depend on the processing conditions of the raw materials from which it is derived like red snapper (lutjnus sp.) [18], sharp nose stingray (Dasyatis Zugei) [12], silver carp (hypophthalmichthys matrix) scales [19], chicken skin [20], small-spotted catshark (S canicular) [21], guina pig [22], "Kacang" goat skin [23] and the method used in the extraction process with or without telopeptides [20], acid soluble and pepsin soluble methods, hydrolysate extraction from chromed leather wastes [1,24]. Thus, it is necessary to determine the appropriate extraction process for each raw material in order to obtain the best performance and the best collagen characteristics.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, it is necessary to determine the appropriate extraction process for each raw material in order to obtain the best performance and the best collagen characteristics. Collagen can be extracted from skin/hide by chemical hydrolysis and enzymatic hydrolysis [25,19]. The enzymatic processes generate less waste; however, it is costly and need a longer time for its effectiveness [25].…”

Section: Introductionmentioning

confidence: 99%

“…The enzymatic processes generate less waste; however, it is costly and need a longer time for its effectiveness [25]. Two stage fractionation procedure using dilute trichloro acetic acid and ethanol is developed for isolation and purification of soluble collagen from crude extracts [19]. Purified collagen must have pH range of 6.0 and 7.0 and the ash content should be less than 0.1% to avoid degradation further.…”

Section: Introductionmentioning

confidence: 99%

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Optimization of Collagen Extraction from Sheep Raw Trimming Wastes Using Acid Hydrolysis

Wakjira¹,

Hunde²,

Balcha³

et al. 2022

JEECE

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Although leather industry plays a significant role in the global economy, it has been categorized as one of highly polluting industries due to its generation of huge amount liquid and solid wastes. Large amount of solid and liquid wastes is generated from tanning industries during leather manufacturing process. These wastes bring about various problems to the environment and human health. Tannery wastes contain significant amount of raw skin wastes that are produced in hide/leather trimming process. The recycling and use of these raw skin/hide wastes (trimming wastes) is very important from environmental as well as economic point of views. The aim of this work was to investigate production of collagen from sheep skin trimming waste. The trimming waste was first pre-treated and then acetic acid hydrolysed to extract collagen. The extracted collagen was characterized using Fourier Transform Infrared (FTIR), UV-spectrometer and Scanning Electron Microscope (SEM). Response Surface Methodology (RSM) was used to optimize collagen extraction parameters (acetic acid, mixing ratio and extraction time). A three-factor, three-level Box-Behnken Design (BBD) based RSM was applied to determine the optimal conditions to obtain maximum collagen yield. A maximum collagen yield of 25.75% was obtained at optimum conditions (acetic acid concentration of 0.54 M, skin to acetic acid ratio of 0.03 g/ml and extraction time 3.33 day) using the RSM. Under these optimum conditions, experimental determined collagen yield of acid-soluble collagen was 25.85% which is in good agreement with the predicted value.

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“…Owing to the ionic bonds, hydrogen bonds, vander Waals bonds, and hydrophobic bonds between molecules [5] , it is difficult for collagen to be dissolved in water or conventional solvent. At present, soluble collagen could be mainly dissolved in acid solution [6] , neutral salt solution [7] , and ionic liquids [8] . These complex solvent systems limit the processing of collagen-based materials.…”

Section: Introductionmentioning

confidence: 99%

Structure and stability analyses of collagen hydrolysate coacervates triggered by ethanol in aqueous solution

Liu

Zhang

et al. 2020

J of Applied Polymer Sci

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The coacervation of collagen hydrolysate (CH) in aqueous solution was triggered by ethanol as poor solvent which has a significant effect on the aggregation and rearrangement of CH macromolecules. In this work, the static coacervation was performed to investigate the influences on coacervates morphology. CH concentration and ethanol temperature had significant influences on coacervates morphology. Treatment for the CH solution of high concentration by lower temperature ethanol (<25°C) tended to form the microspheres morphology. High temperature ethanol was not conducive to CH coacervation, while enhanced the CH solubilization in water‐ethanol. By directly mixing CH solution and ethanol under agitation, dispersed nanospheres could be successfully obtained in suspension. The turbidity and absorbance tests were carried out to further study the CH coacervation behaviors. The stability of milky suspension induced by ethanol was evaluated by a self‐built light transmittance measurement. The result showed that the absorbance and turbidity of CH suspension increased with increasing the VEtOH ratio and CH concentration. The milky suspension with high VEtOH would turn clear gradually due to the CH solubilization in water–alcohol. The maximum absorbance presented at pH around 7 where the charges of CH molecules were negative. The coacervation behaviors of CH were very different from that of collagen and gelatin, owing to its lower molecular weight.

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

Cited by 18 publications

References 28 publications

Production of Hydrolyzed Collagen from Common Carp Cyprinus carpio L. Scales by Synergistic Enzyme Systems

Production of Hydrolyzed Collagen from Common Carp Cyprinus carpio L. Scales by Synergistic Enzyme Systems

Optimization of Collagen Extraction from Sheep Raw Trimming Wastes Using Acid Hydrolysis

Structure and stability analyses of collagen hydrolysate coacervates triggered by ethanol in aqueous solution

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