Development of industrial ultrasound system for mass production of collagen and biochemical characteristics of extracted collagen

Song, Kyung‐Mo; Jung, Sung Keun; Kim, Young Ho; Kim, Young Eon; Lee, Nam Hyouck

doi:10.1016/j.fbp.2018.04.001

Cited by 30 publications

(18 citation statements)

References 17 publications

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“…However, the yield was comparable with collagen from the different scales, spotted golden goatfish (1.66%), seabass (1.44%) and golden carp (1.58%) (Ali et al, 2017;Chuaychan et al, 2015;Matmaroh et al, 2011). The yield might be enhanced by ultrasound assisted extraction via due to mechanical and cavitation effect of ultrasound (Ali et al, 2018;Song et al, 2018;Tu et al, 2015). Song et al (2018) reported that the ultrasound assisted extraction could enhanced the yield of collagen by 1.5-2 times of that obtained by conventional extraction.…”

Section: Yield Of Collagenmentioning

confidence: 85%

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Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale

et al. 2019

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In Thailand, the production of tilapia is about 140,000 tons, which is the sixth tilapia production in the world. From the processing, the scale was generated as waste. To produce a value-added product, the production of collagen from tilapia scale could be an alternative. Generally, collagen from fish scale possesses a less fishy odor and flavor than that from fish bone and skin. From the results, the fish scale is an interesting alternative source for collagen extraction. The objectives of this study were to extract collagen from Nile tilapia (Oreochromis niloticus) scale from the production of frozen tilapia fillet as well as to study its properties. Extraction of acid (ASC) and pepsin soluble collagens (PSC) from Nile tilapia scale, as well as the determination of their yield, amino acid compositions, SDS-PAGE patterns, FTIR spectra, thermal denaturation temperature (Tmax) and zeta potential, was conducted. ASC and PSC had a yield of 0.77 and 0.71% based on dry basis), respectively. The major amino acid found in both collagens was glycine (322-332 residues/1000 residues). Also, they had a high amount of imino acid (199-205 residues/1000 residues). Based on SDS-PAGE pattern, both collagens were classified as type I collagen ((α1)2α2-heterotrimer). The similar FTIR spectra of both collagens were found. Their amide peaks had no shift in wavenumber. ASC and PSC had Tmax of 36.15 and 34.70 °C, respectively. From zeta potential analysis, ASC and PSC had the zero of net chart at pH 5.09 and 5.84, respectively. Based on the characteristics of the collagen, the scale could be an alternative source for collagen production, however their yield should be improved to serve as a potential source for further application.

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Section: Yield Of Collagenmentioning

confidence: 85%

“…The yield might be enhanced by ultrasound assisted extraction via due to mechanical and cavitation effect of ultrasound (Ali et al, 2018;Song et al, 2018;Tu et al, 2015). Song et al (2018) reported that the ultrasound assisted extraction could enhanced the yield of collagen by 1.5-2 times of that obtained by conventional extraction.…”

Section: Yield Of Collagenmentioning

confidence: 99%

Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale

et al. 2019

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“…Thus ISP is a suitable method for recovery proteins from SPBs and microalgae and has advantages, such as the process being simple and scalable to pilot and industrial scales for different SPBs and microalgae [342,343]. Since the process can be conducted under mild conditions (4 • C, pH 6.5-11.5), recovered proteins are if high quality and can be used for the production of functional food [344], functional ingredients [345] or nutraceutical components [344].…”

Section: Isoelectric Solubilisation/precipitation (Isp) Process For Imentioning

confidence: 99%

Protein Recovery from Underutilised Marine Bioresources for Product Development with Nutraceutical and Pharmaceutical Bioactivities

2020

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The global demand for dietary proteins and protein-derived products are projected to dramatically increase which cannot be met using traditional protein sources. Seafood processing by-products (SPBs) and microalgae are promising resources that can fill the demand gap for proteins and protein derivatives. Globally, 32 million tonnes of SPBs are estimated to be produced annually which represents an inexpensive resource for protein recovery while technical advantages in microalgal biomass production would yield secure protein supplies with minimal competition for arable land and freshwater resources. Moreover, these biomaterials are a rich source of proteins with high nutritional quality while protein hydrolysates and biopeptides derived from these marine proteins possess several useful bioactivities for commercial applications in multiple industries. Efficient utilisation of these marine biomaterials for protein recovery would not only supplement global demand and save natural bioresources but would also successfully address the financial and environmental burdens of biowaste, paving the way for greener production and a circular economy. This comprehensive review analyses the potential of using SPBs and microalgae for protein recovery and production critically assessing the feasibility of current and emerging technologies used for the process development. Nutritional quality, functionalities, and bioactivities of the extracted proteins and derived products together with their potential applications for commercial product development are also systematically summarised and discussed.

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“…In recent years, ultrasonic pulses have been used as an environmentally-friendly technology to improve the functional properties of vegetable and animal proteins by altering their hydrogen bonds and hydrophobic interactions, as well as by disrupting their molecular conformation through cavitation, heating, dynamic agitation and shear stress [1]. Additionally, this technology has been used in green chemistry as a tool for the extraction of functional compounds with an improved yield, short time, low cost, and less solvent [2].…”

Section: Introductionmentioning

confidence: 99%

“…High-intensity ultrasound pulses have been tested for collagen extraction at an industrial level, and favorable results were obtained because it was possible to minimize the extraction time (from 24 to 3 h) and acid concentration (from 0.5 to 0.05 M) while obtaining twice the yield compared to the conventional method. The industrial system for this process consists of a collagen separation device (where ultrasound is generated and collagen is separated from the sample), a cooling unit, sample supply, a discharge pipe, and circulation pump [2].…”

Section: Introductionmentioning

confidence: 99%

High-Intensity Ultrasound Pulses Effect on Physicochemical and Antioxidant Properties of Tilapia (Oreochromis niloticus) Skin Gelatin

Cuevas-Acuña¹,

Arias‐Moscoso²,

Torres‐Arreola³

et al. 2020

Applied Sciences

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Ultrasonic pulses are considered green technology for the improvement of the functional properties of proteins. In this study, four high-intensity ultrasound pulse treatments (ultrasound-pulsed gelatin (UPG)-42, UPG-52, UPG-71, UPG-84, and non-pulsed control gelatin (CG)) were applied to tilapia (Oreochromis niloticus) skin gelatin in order to study their effect on its physicochemical and antioxidant properties; a non-treated gelatin was used as a control. UPGs showed a significant increase in soluble protein and surface hydrophobicity compared to the control gelatin, and no significant difference was found in the electrophoretic profiles. The effects on the secondary structure were studied by circular dichroism and infrared spectra, and these showed that the random coil conformation was the main component in all treatments and the ultrasonic treatments only affected the α-helix and β-sheet proportion. Finally, the ABTS ((2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)) and FRAP (ferric reducing ability) assays demonstrated that ultrasound treatments could improve the antioxidant activity of gelatins as free radical scavengers and electron donors. These results suggest that high-intensity ultrasound pulse technology is useful to improve fish gelatin antioxidant properties, which could be associated with secondary structure disruption.

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Development of industrial ultrasound system for mass production of collagen and biochemical characteristics of extracted collagen

Cited by 30 publications

References 17 publications

Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale

Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale

Protein Recovery from Underutilised Marine Bioresources for Product Development with Nutraceutical and Pharmaceutical Bioactivities

High-Intensity Ultrasound Pulses Effect on Physicochemical and Antioxidant Properties of Tilapia (Oreochromis niloticus) Skin Gelatin

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