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Extraction techniques, structural features, and functional properties of collagenous derivatives from unconventional animal sources: a review
(2026-12-01)
Indriani, Sylvia
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Petcharat, Tanyamon
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Andriani, Cynthia
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Benjakul, Soottawat
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Nalinanon, Sitthipong
Collagenous derivatives (collagen, gelatin, and collagenous hydrolysate (CH)) are extensively used across the food, biomedical, and pharmaceutical industries. Traditionally, these have been sourced from porcine, bovine, and fish due to their ready availability and biocompatibility. However, conventional collagenous derivatives face ongoing challenges regarding sustainability, resource intensity, and socio-cultural perceptions. This has led to the exploration of alternative collagenous derivatives from unconventional sources, with a primary focus on evaluating their potential for yields, extractability, and functional properties, all of which are fundamental for future scale-up and alternative applications. This review summarizes alternative collagenous derivatives from unconventional animals, including amphibians, mollusks, echinoderms, insects, unconventional fish and byproducts, and reptiles. Their structures, extraction techniques, functional properties, and potential applications are comprehensively summarized, showcasing their ability to complement or even surpass conventional sources in specific uses. Additionally, the challenges and prospects for industrial application, emphasizing the sustainability of meeting growing collagen demand and encouraging further research into these promising alternative sources, were discussed. Unconventional collagenous derivatives demonstrate excellent and unique characteristics as alternatives to conventional ones. Type I collagen from amphibians, reptiles, and mollusks had superior thermal stability. Unconventional gelatin and CH also possess various bio-functionalities that can enhance their potential applications. The relatively low extraction yield could be addressed by increasing the concentration of chemicals or extraction time and incorporating green technology without causing an adverse impact on the quality. These findings indicate the potential applications of unconventional collagenous derivatives as food ingredients and supplements.
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Ultrasonication on Collagen Yield, Physiochemical and Structural Properties from Seabass (Lates Calcarifer) Scales as Affected by Pretreatment and Extraction Conditions
(2024-01-01)
Bavisetty, Sri Charan Bindu
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Karnjanapratum, Supatra
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Dave, Jaydeep
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Purba, Daniel Tua
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Kudre, Tanaji
This research explored the use of ultrasound as a pretreatment and extraction assisted process for extraction of collagen from seabass scales. Both acid-soluble (AC) and pepsin-soluble collagens (PC) were extracted with ultrasonication at different extraction times (24 and 48 h). Ultrasound pretreatment (PU) and ultrasound-assisted extraction (UE) notably improved AC extraction yields over 48 hours, registering 2.12% and 4.62%, respectively. The highest yield for PC, 21.85%, was achieved with 48 hours of ultrasound assisted extraction. Protein analysis verified the extracted collagens as type I, indicated by the presence of specific α and β chains. Further, FTIR spectra confirmed collagen's presence in all samples through distinct amide band peaks. Interestingly, ultrasound processes marginally reduced AC's thermal stability while boosting PC's thermal stability, especially when combined with pepsin treatment. Moreover, CD spectroscopy showed the preserved native structure of collagen across all samples. The ultrasound method increased collagen extraction yields and retained its structural integrity. These outcomes are pivotal for advancing collagen extraction methods in the biomedical and food sectors.
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Meat quality, post-mortem proteolytic enzymes, and myosin heavy chain isoforms of different Thai native cattle muscles
(2021-09-01)
Chaosap, Chanporn
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Sivapirunthep, Panneepa
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Sitthigripong, Ronachai
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Tavitchasri, Piyada
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Maduae, Sabaiporn
Objective: This study investigated the meat quality characteristics, endogenous proteolytic enzymes, collagen content, and myosin heavy chain (MyHC) isoforms of different muscles of Thai native cattle (TNC). Methods: Infraspinatus (IF), Longissimus thoracis (LT), and Supraspinatus (SS) muscles were obtained from two TNC breeds, Kho-Lan (KL, n = 7) and Kho-Isaan (KI, n = 7). The muscle and meat characteristics of TNC breeds and their relationship with MyHC expression were examined. Results: Three MyHC isoforms namely MyHC I, MyHC IIa, and MyHC IIx were detected in the muscles. The KL had higher (p<0.05) MyHC IIx than the KI. The IF muscle had higher (p<0.05) MyHC I compared to other muscles. The LT muscle had the least MyHC I. The LT had higher (p<0.05) MyHC IIx than the IF and SS muscles. The IF presented the least MyHC IIx. The KL had higher (p<0.05) lightness and moisture content and lower crude protein, redness, cooking loss, shear force, and calpastatin than the KI. The glycogen, total collagen, soluble collagen, crude protein, ash contents, and troponin T degradation product of IF and SS were lower (p<0.05) than that of LT. Ether extract in LT was lower (p<0.05) than that of IF and SS. The percentage of MyHC I, MyHC IIa, and MyHC IIx were significantly correlated with muscle and meat characteristics of TNC. Conclusion: These results suggest that the differences in the MyHC isoforms may partly account for the variation in meat quality between breeds and among muscles of TNC.
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Carcass composition, meat quality, calpain activity, fatty acid composition and ribonucleotide content in southern thai native goats and three-way crossbred goats
(2021-06-01)
Chaosap, Chanporn
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Chauychuwong, Nantana
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Chauychuwong, Ratchasak
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Sriprem, Chatchai
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Sivapirunthep, Panneepa
Carcass composition, meat quality, calpain activity, fatty acid composition, and ribonucleotide content were examined and compared between male Southern Thai native goats (NG, n = 10) and three-way crossbred goats (CG, 50% Boer × 25% Saanen × 25% Southern Thai native, n = 10). All animals were fed 1.5% body weight of concentrate (16% protein and 70% total digestible nutrients) and fresh Napier grass for 4 months. At the end of raising period, the final weight between the two genotypes was not significantly different. The percentage of carcass, bone, and fat of CG were higher than those of NG. NG presented lower shear force values, insoluble and total collagen content but higher collagen solubility and calpain-1 activity at 24 h postmortem. Additionally, NG meat was high in monounsaturated fatty acids but low in saturated fatty acids. However, the amount of ribonucleotide was no significant difference between two genotypes.
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Myosin heavy chain isoforms expression, calpain system and quality characteristics of different muscles in goats
(2020-08-15)
Chaosap, Chanporn
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Sitthigripong, Ronachai
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Sivapirunthep, Panneepa
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Pungsuk, Apichaya
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Adeyemi, Kazeem D.
Myosin heavy chain (MHC) isoforms in goat muscles and their possible relationships with meat quality have not been fully elucidated. This study characterized the MHC isoforms in different caprine muscles using sodium dodecyl sulphate glycerol gel electrophoresis (SDS-GGE). The relationships between MHC isoforms, calpain systems and meat quality characteristics of different muscles in goats were examined. Four muscles, namely infraspinatus (IF), longissimus dorsi (LD), psoas major (PM) and supraspinatus (SS) were obtained from ten Boer crossbred bucks (7–10 months old; 26.5 ± 3.5 kg, BW). The percentages of MHC I, MHC IIa and MHC IIx in SS, IF, PM and LD were 47.2, 38.3, 32.1, 11.9; 28.0, 42.1, 33.0, 36.4; and 24.8, 19.6, 34.9 and 51.7, respectively. IF and SS had higher levels of calpastatin, total collagen and insoluble collagen contents than did PM and LD. PM had longer sarcomere length than did other muscles. LD had higher collagen solubility, troponin-T degradation products and glycogen content than did other muscles. These results infer that variable fiber-type composition could account partially for the differences in the physicochemical properties of goat muscles.
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Characterization of acid soluble collagen from the skin of snakeskin gourami (Trichogaster Pectoralis)
(2020-01-01)
Sukkon, Piyaporn
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Ali, Ali Muhammed Moula
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Nalinanon, Sitthipong
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Kishimura, Hideki
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Takeungwongtrakul, Sirima
The present study was aimed to isolate and characterized acid soluble collagen (ASC) from the skin of snakeskin gourami (Trichogaster pectoralis). ASC from gourami skin had a yield of 9.43% and 34.65%, based on wet and dry weight basis, respectively. The purity of ASC was superior with a distinct absorption peak at wavelength (WL) of 230.7 nm. Based on the electrophoretic pattern, gourami skin ASC was classified as type I collagen, as it comprised α1 and α2 as major components and higher molecular weight (MW) components γ, β were distinctly observed. ASC exhibited high Tmax value of 33.43°C, which could correspond to its imino acids content of 188 residues/1000 residues. Fourier transform infrared (FTIR) spectrum and circular dichroism (CD) revealed that ASC extracted from gourami skin had greater structural integrity in its triple-helical form. Solubility of ASC was high at the pH range of 2-4 in which zeta potential exhibited highly positive charge. The highest solubility of ASC in the presence of NaCl was observed at 2% (w/v). Therefore, with all the characteristic features, ASC from snakeskin gourami skin can be a valueadded product in the fish processing industry.

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