Characterization of the Acid- and Pepsin-Soluble Collagens from Haruan (Channa striatus) Scales

Indrati, Retno; Pamungkas, Bagus Fajar; Supriyadi, Supriyadi; Murdiati, Agnes

doi:10.3923/pjn.2019.324.332

Cited by 4 publications

(7 citation statements)

References 39 publications

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“…Meanwhile, the solubility of collagen decreased gradually with increasing NaCl concentration and sharply decreased when the NaCl concentration was 4% ( w / v ), after which the solubility remained constant at a low level until 6% ( w / v ). The results were comparable to the solubility of collagen from barramundi skin ( Lates calcarifer ) by Jamilah et al [ 35 ] and haruan scales ( Channa striatus ) by Pamungkas et al [ 20 ]. A higher concentration of NaCl may result in decreased protein solubility via a “salting out” effect by increasing hydrophobic interaction between protein chains and increasing competition for water with ionic salts, resulting in protein precipitation [ 20 , 34 ].…”

Section: Resultssupporting

confidence: 85%

“…In this study, before being digested, the fish skin was hydrolysed or treated with acetic acid, followed with pepsin enzymes to remove telopeptides. The enzyme functioned by crosslinking collagen’s non-helical ends (telopeptides) [ 23 ], deleting intermolecular bonding even when they were most stable in acidic solution without causing damage to the triple helix, and therefore increasing collagen solubility in acid medium [ 20 ].…”

Section: Resultsmentioning

confidence: 99%

“…According to Nalinanon et al [ 34 ], pepsin was able to break the telopeptide regions’ nonhelical section, hence increasing the amount of PSC’s helical structure stabilised by the H-bond. Amide III peaks included absorption induced by CH 2 wagging vibrations in the glycine backbone and proline sidechains, as well as C–N stretching vibrations and N–H deformation caused by amide links [ 20 ]. ASC and PSC amide III peaks were seen at 1242 cm −1 and 1240 cm −1 .…”

Section: Resultsmentioning

confidence: 99%

“…The influence of pH on collagen solubility is related to the protein’s isoelectric point (pI): the point at which the protein’s total charge approaches zero [ 35 ]. However, solubility continued to rise with rising pH in the alkaline pH range of 7 to 10, owing to the neutralising effect of the collagen molecules [ 20 ]. This is due to the increased hydrophobic–hydrophobic interaction between collagen molecules, resulting in a total net charge of zero, particularly at pI [ 23 ].…”

Section: Resultsmentioning

confidence: 99%

“…In addition, according to Yu et al [ 19 ] who optimised three critical parameters for the pepsin soluble collagen (PSC) extraction method: pepsin concentration at 1389 U/g, hydrolysis time (8.67 h) and solid–liquid (S/L) ratio of 1:57 produced a yield of 84.85%. Pepsin acts by cleaving crosslinked regions within the telopeptide without causing damage to the triple helix and increasing collagen solubility in acid [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Acid- and Pepsin-Soluble Collagen Extracted from the Skin of Purple-Spotted Bigeye Snapper

Oslan

Shapawi

Mokhtar

et al. 2022

Gels

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Fish processing waste is a prospective source of collagen and a cost-effective environmental pollutant. The skin of the purple-spotted bigeye snapper (Priacanthus tayenus) was extracted utilising various acid soluble collagens (ASC) including acetic acid (AAC), lactic acid (LAC), citric acid (CAC) and pepsin soluble collagens (PSC). In this study, PSC (6.65%) had the highest collagen yield, followed by AAC (5.79%), CAC (4.15%), and LAC (3.19%). The maximum temperatures (Tmax) denaturation of AAC, LAC, CAC, and PSC were 31.4, 31.7, 31.5, and 33.2 °C, respectively. UV-VIS absorption spectra showed all extracted collagens had a range of absorbance at 230 nm, due to the presence of glycine, proline, hydroxyproline, and triple-helical collagen. Additionally, they exhibited amide A, B, amide I, II, and III peaks. SDS–PAGE identified all extracted collagens as type I. The PSC had a significantly higher (p < 0.05) hydroxyproline content than acidic extraction 66.3 ± 1.03 (mg/g sample). Furthermore, all samples were extremely soluble in acetic conditions at pH 5, and all collagen was soluble in NaCl up to 3% (w/v). Therefore, PSC was the best treatment since it did not impact collagen triple helical and acetic acid yielded the most collagen in ASC extraction. Overall, the analysis revealed that fish skin waste might be used as an alternate source of collagen in diverse applications, particularly in food applications.

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Section: Resultssupporting

confidence: 85%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Characterization of Acid- and Pepsin-Soluble Collagen Extracted from the Skin of Purple-Spotted Bigeye Snapper

Oslan

Shapawi

Mokhtar

et al. 2022

Gels

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Extraction of proteinaceous components and biominerals from cold water fish fileting side streams: a review

Kendler,

Sasidharan,

Rustad

2024

Front. Sustain. Food Syst.

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Fileting is a popular form of processing methods and in addition to being sold fresh or frozen, filets are used for preparation products battered and breaded filets. This generates considerable amount of side streams like skin, frames, and cut-offs which forms around 30–70% of the total body weight. The European Waste Framework Directive 2008 and recent amendments [EU WFD (2018/851)] stipulates comprehensive regulations which the manufacturers must follow while handling the side streams generated during the processing. This demands a detailed compilation of information regarding the yield, classification and valorization potential of side streams associated with the fileting operations of the cold-water finfishes. The side streams are a rich source of proteins including structural proteins like collagen and biominerals such as hydroxyapatite which find multiple application in food and pharmaceutical industry. Previously, the recovery of these components was performed by extensive chemical treatment with acids or bases, including subsequent washing steps. Nowadays, green extraction methods, defined as technologies with reduced energy and chemical consumption, should be considered to achieve a green shift in the food industry. Nevertheless, industrial upscaling of green extraction methods and subsequent refinement of the isolated compounds must be further evaluated and improved in order to achieve a green shift in food industry by using side-stream derived compounds as ingredients. Moreover, legislations as well as national and international regulations must be considered and evaluated. Even though a number of articles are recently available regarding seafood side stream valorization, this review focus on side streams generated predominantly from cold water fish species and also discusses sustainable green technologies to be included during the recovery process.

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Biochemical Characteristics of Acid-Soluble Collagen from Food Processing By-Products of Needlefish Skin (Tylosurus acus melanotus)

et al. 2022

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The by-product of needlefish (Tylosurus acus melanotus) waste possesses important characteristics that could be used in food applications. Fish by-product collagen may be used in place of mammalian collagen due to ethical and religious considerations over environmental degradation. Different forms of acid-soluble collagen (ASC) were successfully extracted from needlefish skin. Based on dry weight, the collagen extracted using acetic acid (AAC), lactic acid (LAC), and citric acid (CAC) treatments was 3.13% with a significantly difference (p < 0.05), followed by 0.56% and 1.03%, respectively. Based on proximate analysis, the needlefish skin composition was found to be significantly different (p < 0.05) between compositions, with the highest moisture content at 61.65%, followed by protein (27.39%), fat (8.59%), and ash (2.16%). According to the SDS-PAGE results, all extracted collagen were identified as a type 1 collagen. Additionally, ATR-FTIR revealed that all collagens had amide A, B, amide I, II, and III peaks. AAC significantly outperforms LAC and CAC in terms of yield following physicochemical characterisation, including pH determination, colour (L* value), and hydroxyproline content. All collagens demonstrated strong heat resistance and structural stability with Tmax above 38 °C. Collagen was most soluble at pH 5 for AAC, pH 3 for LAC, and pH 7 for CAC. The effect of collagen solubility on NaCl concentration was discovered to be significantly reduced to 50 g/L for all collagen samples. All collagens can be used as alternatives to terrestrial collagen in a diverse range of applications.

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Characterization of the Acid- and Pepsin-Soluble Collagens from Haruan (Channa striatus) Scales

Cited by 4 publications

References 39 publications

Characterization of Acid- and Pepsin-Soluble Collagen Extracted from the Skin of Purple-Spotted Bigeye Snapper

Characterization of Acid- and Pepsin-Soluble Collagen Extracted from the Skin of Purple-Spotted Bigeye Snapper

Extraction of proteinaceous components and biominerals from cold water fish fileting side streams: a review

Biochemical Characteristics of Acid-Soluble Collagen from Food Processing By-Products of Needlefish Skin (Tylosurus acus melanotus)

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