Content area
One of the challenges in the tuna processing industry is waste management. Tuna skin is a byproduct rich in protein and has great potential for collagen. This study aimed to extract collagen from tuna skin waste (Thunnus sp.) and apply it in citrus honey tea (yujacha) beverage as a functional food product. Collagen extraction was carried out using the hydro-extraction method. Characterization included proximate analysis collagen content (using Fourier Transform Infrared test), antioxidant activity (using the Ferric Reducing Antioxidant Power method), and amino acid composition (using high performance liquid chromatography). The production of collagen drinks was carried out with four treatments of collagen concentration (0, 1, 2, and 3%) to assess its effect on viscosity, pH, and hedonic quality. The results showed that the collagen produced had a high protein content (86.55%), low moisture content (7.02%), and ash content (0.67%), which was in accordance with SNI standards. The collagen exhibited high antioxidant activity, measuring 151.65 pmol Fe? gi. The amino acids content was dominated by glycine, proline, and arginine. The application of collagen in yujacha beverages increased viscosity (26.11-38.60 cP) and pH (3.26-4.26), although there was a decrease in sensory receptivity to aroma and taste with an increased collagen concentration. This study concluded that collagen from tuna skin waste has a great potential as an innovative raw material for functional food products, especially beverages. In addition to increasing the added value of fishery waste, these results support the development of high economic value and sustainable products in the food industry.
Abstract. One of the challenges in the tuna processing industry is waste management. Tuna skin is a byproduct rich in protein and has great potential for collagen. This study aimed to extract collagen from tuna skin waste (Thunnus sp.) and apply it in citrus honey tea (yujacha) beverage as a functional food product. Collagen extraction was carried out using the hydro-extraction method. Characterization included proximate analysis collagen content (using Fourier Transform Infrared test), antioxidant activity (using the Ferric Reducing Antioxidant Power method), and amino acid composition (using high performance liquid chromatography). The production of collagen drinks was carried out with four treatments of collagen concentration (0, 1, 2, and 3%) to assess its effect on viscosity, pH, and hedonic quality. The results showed that the collagen produced had a high protein content (86.55%), low moisture content (7.02%), and ash content (0.67%), which was in accordance with SNI standards. The collagen exhibited high antioxidant activity, measuring 151.65 pmol Fe? gi. The amino acids content was dominated by glycine, proline, and arginine. The application of collagen in yujacha beverages increased viscosity (26.11-38.60 cP) and pH (3.26-4.26), although there was a decrease in sensory receptivity to aroma and taste with an increased collagen concentration. This study concluded that collagen from tuna skin waste has a great potential as an innovative raw material for functional food products, especially beverages. In addition to increasing the added value of fishery waste, these results support the development of high economic value and sustainable products in the food industry.
Key Words: extraction, characteristics, collagen, tuna skin, collagen drink.
Introduction. One of the biggest challenges in the fish processing industry is tuna waste, which is often not managed properly, potentially causing environmental problems (Rahantan et al 2024). Tuna waste consists of 17% head, 8% skin, 5% innards, 4% bones, and 2% fins (Hursepuny et al 2021). One way to optimize the use of tuna fish skin waste is to process it into collagen, which has high economic value (Sembiring et al 2020). According to Ardhani et al (2019), tuna skin is rich in protein so it has great potential as a source of collagen. The complex structural proteins found in fish skin play an important role in maintaining the strength and flexibility of various body parts such as skin, ligaments, bones, joints, muscles, tendons, gums, eyes, blood vessels, nails and hair. Collagen can be extracted with acids and enzymes or even a combination of both (Alhana et al 2015). In addition, collagen extraction can be done using the acid-hydroxy-extraction method (Kusa et al 2022). The acid-hydroxy-extraction method has several advantages including shorter time, requires little laboratory equipment, can be produced continuously, with a high yield, little waste and lower production costs (Huang et al 2016).
Collagen is a connective tissue protein that can be obtained from fish skin waste. (Nurjanah et al 2021). Collagen has a fibrous structure which is the main component of the extracellular matrix of a living organism with an amount ranging between 25 to 30% of the total protein and plays an important role in maintaining the integrity of the biological structure of several tissues (Hema et al 2013). The amino acid composition of collagen is mainly composed of glycine, proline, and alanine, which form a triple helix structure consisting of three a chains.
The amino acid composition and physicochemical characteristics of collagen can vary greatly, depending on the type of tissue in which it is found (Hema et al 2013). Collagen is a major substance in living cells and plays an important role in cellular homeostasis (El Blidi et al 2021). Collagen can help wound healing (Ibrahim et al 2020). Amino acids in collagen can increase fibroblast proliferation, strengthen skin tissue and increase the synthesis of natural collagen fibers in the skin so that it is very useful in accelerating wound healing (Afifah et al 2019; Kong et al 2023). Collagen has an effective antioxidant effect in counteracting the accumulation of free radicals in the skin so that it has the potential as an anti-aging due to oxidative stress caused by exposure to UV rays (Devita et al 2021). According to Wang et al (2013), collagen derived from fishery waste is widely used in functional foods and beverages due to the functional properties of collagen. Functional beverages provide a healthy effect when consumed because they are rich in nutrients. As functional foods and beverages, they must fulfill two main functions, namely providing nutritional intake and sensory satisfaction such as good taste and good texture (Widyantari 2020). Collagen drinks contain collagen extract mixed with various additional ingredients to enhance its taste. Collagen drinks have been widely traded because many people are interested in their benefits.
One of the uses of collagen that can be developed and increase added value is the addition of collagen as a wound healer, protein source, and antioxidant in beverage products. This study aimed to determine the quality characteristics of raw materials, namely: tuna (Thunnus sp.) skin collagen and yujacha collagen drinks, and the effect of adding tuna skin collagen to yujacha drinks.
Material and Method
Materials and tools. The main raw material used was tuna skin (Thunnus sp.) that came from tuna processing waste. The chemicals used were NaOH (Brand, Germany), СНЗСООН (Brand, Germany), and distilled water. The tool used was a pH meter (JENWAY 3520), Fourier Transform Infrared Spectroscopy (UV1800 V/VIS), Freeze dryer (Telstar LyoQuest), and Viscotester VT - 04F (Rion Ltd., China).
Collagen extraction. The extraction process of collagen using the hydro-extraction method refers to the method of Afifah et al (2023), which was modified.
Making drink citrus honey tea (yujacha). The manufacture of yujacha drinks refers to Bilek & Baryam (2015). The collagen concentration treatment consists of four different collagen concentrations. The formulation of each treatment can be seen in Table 1.
Test of physicochemical characteristics of collagen. The collagen extracted was then tested for physicochemical characteristics with the parameters: proximate content, collagen content (via Fourier Transform Infrared Spectroscopy (FTIR)), amino acid composition, and antioxidant activity. The proximate quality test was carried out in the form of moisture content (Indonesian National Standard 2015), ash content (Indonesian National Standard 2010), protein content (Indonesian National Standard 2006), and fat content (Indonesian National Standard 2017). The FTIR test refers to Kristoffersen et al (2023). The analysis of the composition of collagen amino acids refers to AOAC (2005). Testing of antioxidant activity was carried out using the FRAP (Ferric Reducing Antioxidant Power) method referring to Wahyudi et al (2022).
Quality test of citrus honey tea (yujacha) drink. Citrus honey tea (yujacha) drinks were tested for quality with hedonic, pH, and viscosity parameters. Hedonic quality testing was carried out by 30 panelists with reference to Adrianar et al (2015). The pH measurement was performed according to AOAC (2005). Viscosity testing was carried out according to Maharani (2018).
Data analysis. The experiment used is a one-way, one group, randomized design. The data was processed by analysis of variance (ANOVA) and Kruskal Wallis using IBM 22 SPSS.
Results and Discussion
Chemical composition of collagen. The analysis of collagen's characteristics was carried out to find out the special properties of collagen. The quality characteristics tested were chemistry, FTIR functional group components, amino acids, and antioxidants. The results of the tuna skin collagen chemical test are presented in Table 2.
The moisture content of the collagen produced was 7.02%. This value is in accordance with the SNI 8079:2020 (Indonesian National Standard 2020), which is <14%. The moisture content of collagen from the results of this study are lower than tuna skin collagen from the research of Hema et al (2013), where it was 7.5%. However, it is higher than in the research of Kusa et al (2022), where it was of 1.91%, and in the research of Suptijah (2018), where it was of 6.55%. Collagen in this study has a low moisture content, allegedly due to the drying procedure carried out using a freeze dryer, while the high-water content can be caused using a high acid concentration. High acid concentrations have a greater and more effective ability to hydrolyze collagen and cause shortening of the collagen peptide chain, thereby increasing the ability of collagen to absorb water (Devi et al 2017). The higher the moisture content in collagen, the lower the collagen's shelf life. Conversely, if the moisture content is low, the collagen's shelf life will be longer (Prestes et al 2013).
The ash content of collagen was 0.67%. This shows that the ash content of collagen from this study was lower when compared to the ash content in Hema et al (2013), of 0.74%, and Suptijah (2018), of 1.80%. The low ash content in collagen indicates that the demineralization process in the pre-treatment stage effectively reduces the minerals contained in tuna skin. The minerals of a material are related to the ash content. According to Suptijah (2018), the ash content in a food ingredient describes the amount of minerals contained in the food ingredient. The quality requirements for collagen for ash content in dry collagen samples are <1% so that the collagen sample is in accordance with the SNI 8079:2020 standard.
The total protein content test result was 86.55%. Total protein content in collagen is higher than the protein content determined by Kusa et al (2022), of 82.96% and by Suptijah (2018), 64.74%, but lower than found by Hema et al (2013), of 91.08%. According to Kusa et al (2022), the total protein content in collagen is proportional to the amount of collagen produced, because protein is the main component in collagen. The protein content and extraction results of collagen will increase as the extraction time increases.
The fat content of the collagen was 2.92%. The collagen fat content is higher when compared to the collagen of 0.74% found by Kusa et al (2022) and of 0.64% by Hema et al (2013), and lower than in Suptijah (2018), namely of 8.85%. The presence of fat in tuna skin is a contaminant that must be removed at the pre-treatment stage, because fat and minerals can reduce the effectiveness of collagen use in various products (Shon etal 2011).
The collagen function group with FTIR. Fourier Transform Infrared Spectroscopy (FTIR) analysis of collagen is used to analyze the secondary structure of the collagen, through the amide bands (bond vibrations of the peptides linking amino acids in protein), such as: Amide A, Amide B, Amide I, Amide II, Amide III, as well as to see collagen crosslinking, and collagen denaturation or damage due to heating. FTIR is an analytical technique commonly used to determine functional groups in a compound. According to Nagarajan et al (2012) if a certain IR frequency is absorbed by an organic compound, vibrations will arise in the organic compound. The characteristics of collagen functional groups are presented in Figure 1.
The following are the characteristics of collagen functional groups resulting from FTIR analysis, which are presented in Table 3.
Figure 1 and Table 3 show the results of the FTIR spectra of collagen. The absorption peaks in the amide absorption region include amides A, B, I, II, III. Tuna fish skin collagen was detected at a wave number of 3,488 cm-1 which is the peak of the amide a group with NH stretching characteristics. According to Shakila et al (2012), the normal wave number for amide A is in the range of 3,490 to 3,430 cm-1. When the NH group in the peptide is affected by hydrogen bonds, its frequency will shiftto a lower direction. Amide A in collagen standards is at 3,490 ст"! because it is influenced by the OH functional group that participates as a water molecule in collagen. According to Utami et al (2024), a wave number of 3,270 cm™ corresponds to the absorption area of the amide A band in the collagen of the swim bladder of the manyung fish, indicating the presence of hydrogen bonds with medium strength (Foggia et al 2011), Amide A found in the collagen of the swim bladder of the giant catfish (Ariidae) is a stretch of NH bound by hydrogen bonds. Amide group В was detected at wave number 2,930 cm'! with the characteristics of СН» asymmetric stretching. Li et al (2013) stated that the absorption region of the amide B group will be detected at wave number 2,915 to 2,935 ст"! with the characteristic properties of CH2 asymmetry of the resulting stretching. According to Utami et al (2024), the wave number of amide B in the collagen of the swim bladder of the manyung fish was detected at a peak of 3,065 cm', which is higher than that of tuna skin collagen, which shows a peak at a wavelength of 2,930 cm. The presence of the amide В group located close to 3,000 cm" indicates the presence of asymmetric stretching of CH2 (Kong & Yu 2007).
Amide I group in collagen was detected in the range of 1,654 cm, which shows the characteristic of C=0 stretching. Amide I group is a typical functional group that forms collagen. The absorption of amide I group is usually detected at wave numbers between 1,600 to 1,690 cm, with the characteristic of C=0 stretching. Amide I is the main differentiator between collagen and other proteins. Amide I has a close correlation with the secondary structure of proteins (Muyonga et al 2004a). The secondary structure spectrum of amide I consists of a-helix in the absorption region of 1,654 cm' and 1,658 cm, Bsheet in the absorption region of 1,624 and 1,642 cm, B-turns in the absorption region of 1,666 cm", 1,672 cm, 1,680 cm? and 1,688 cm, and random coil in the absorption region of 1,648 cm! (Muyonga et al 2004a). Amide I in the collagen standard has a peak at a wavelength of 1,630 cm (Shakila et al 2012). Amide II group in tuna fish skin collagen has an absorption region at 1,552 ст"! with characteristic properties of NH bending, CN stretching. The absorption region of Amide III of tuna skin collagen extraction is 1,237 cm. Kong & Yu (2007) stated that the absorption region of the amide III group in collagen is located in the range between 1,229 to 1,301 cm. The absorption region of amide III indicates the presence of a triple helix structure (Andakke et al 2020).
Amino acid content of collagen. According to Devita et al (2021), the quality of a protein can be assessed from the content of the amino acids that make up the protein. Amino acids contribute to the stability of the collagen helix structure. The amino acid content of tuna skin collagen is presented in Table 4.
The amino acid composition analysis show that the amino acid content of collagen is dominated by: glycine, proline, arginine, alanine and glutamic acid, with levels of 12.89, 6.23, 5.37, 5.68, and 4.42%, respectively, of the total collagen amino acids. Kolanus et al (2019) stated that hydro-extracted collagen from tuna fish skin has a content of glutamic acid, glycine, arginine, alanine and proline of 7.17, 12.25, 5.82, 4.95, and 4.86%, respectively, of the total collagen amino acids. This is in accordance with Hema et al (2013), who stated that the amino acid composition of collagen tends to be dominated by glycine, proline, hydroxyproline and alanine. The results of the study showed that collagen contains 15 types of amino acids, namely eight types of. essential amino acids (phenylalanine, isoleucine, valine, arginine, lysine, leucine, threonine, histidine) and seven non-essential amino acids (i.e. serine, glutamic acid, alanine, glycine, proline, tyrosine, aspartic acid). The higher the content of essential amino acids in food ingredients, the better the quality of the food protein (Jacoeb et al 2012).
Antioxidant activity. The antioxidant activity value of tuna-fishskin collagen is equal to 151.65 pmol Fez gi. This result is higher than the antioxidant activity in catfish skin collagen, which is as large as 20.45 pmol Fe2 д"! (Yanti et al 2022). A molecule's antioxidant capacity is: very strong for values >500 pmol Fez gi, strong for values >100 and <500 pmol Fe2 gi, medium for values >10 and <100 pmol Fez gi and weak for values <10 pmol Fe? gi (Nurjanah et al 2018). Antioxidants are compounds or substances that can be used to protect food by inhibiting damage, rancidity or discoloration caused by oxidation. Antioxidants can act as donors of hydrogen atoms or can act to inhibit free radicals so that they can delay the initiation stage of free radical formation (Tumilaar et al 2024). The addition of collagen to drinks increases the percentage of inhibition. The higher the concentration of collagen, the greater the antioxidant activity value (Permata & Sayuti 2016). This antioxidant analysis was conducted to determine the value of antioxidant activity in collagen after undergoing processing. Antioxidant activity testing using the FRAP method showed that tuna skin collagen has the ability to reduce ferric ions (Fes· to Fe2·), this illustrates that the collagen has antioxidant activity. FRAP reduction capacity testing measures the ability of antioxidant compounds to donate electrons to ferric ions (Fe 3+) to form blue ferrous ions (Fe2·) (Choi et al 2010).
Yujacha collagen drink. The properties of the yujacha collagen drinks that were tested included viscosity, pH, and hedonic quality values. The result of test can be seen in Table 5.
Viscosity of yujacha collagen drink. Based on Table 5, the results obtained are the control sample (without the addition of collagen) yujacha drink has a viscosity of 26.11 cP. Orange juice drinks with collagen concentrations of 1, 2, and 3% respectively have viscosity values of 29.04, 32.94 and 38.60 cP. The addition of collagen at different concentrations increases the viscosity of the fruit juice drink. The viscosity value at a collagen concentration of 3% has a is the highest. Viscosity is the level of thickness of a sample measured in certain units. The higher the viscosity value of a product, the higher the level of thickness (Kumalasari et al 2015). The viscosity of orange juice in Dwiloka et al (2022) had a value of 4.28+0.12 cP, while in Hawa et al (2016) had a value of 0.94 cP. This difference is due to the type of fruit used and to the sensitivity of the viscometer. Viscosity will decrease when the temperature is increased to 32°C because of the hydrogen bond, which provides the stability of collagen structure, is damaged (Yanti et al 2022). On the other hand, increasing collagen concentration causes the viscosity to increase logarithmically. However, viscosity tends to decrease gradually with increasing temperature (FAO 2012). From the results of the analysis of variance, there was a real difference in the treatment because the value (p<0.05). The results of the Tukey test further show a significant difference between the control treatment (0%) and the treatment of collagen addition of 1, 2, and 3%. The treatment with the addition of 1% is significantly different from the treatment of collagen addition of 0, 2, and 3%. The treatment with the addition of 2% is significantly different from the treatment of collagen addition of O, 1, and 3%. The treatment with the addition of 3% is significantly different from the treatment of collagen addition of 0, 1, and 2%.
pH value of yujacha collagen drink. The control sample of citrus honey tea (yujacha) (without the addition of collagen) had a pH value of 3.26, while the yujacha samples with a collagen addition at concentrations of 1, 2 and 3%, respectively, had pH values of 3.47, 3.97 and 4.26. Added collagen increases the pH, while the pH baseline range usually found in fruit juice drinks is 3.0 to 4.0S. Products with a lower pH tend to be more durable because high acidity levels can inhibit microbial growth (Rakhmawati & Yunianta 2015). The higher the acidity level of the fruit, the lower the pH value (Dari & Jumita 2020). The pH value of collagen-fortified yujacha drinks can be seen in Table 5. The ANOVA shows a significant difference among the treatments (p<0.05), further confirmed by the Tukey's test results among treatments (added collagen at 1, 2 and 3%).
Hedonic quality of yujacha collagen drink. The average hedonic quality of yujacha collagen beverages can be seen in Table 5. The hedonic quality parameters tested include appearance, smell, taste, and texture. Parameter scores are determined on a 5-point hedonic scale (Scale: 1-dislike extremely; 2-dislike slightly; 3-neither like nor dislike; 4like slightly; 5-like extremely), one of the most widely used in hedonic tests, being relatively simple and sensitive (Adrianar et al 2015). The values of the appearance parameter are the highest for the control, with a value of 3.80, and the lowest at a collagen concentration of 3%, with a value of 3.53. Appearance is a visual assessment, which is determined mostly by color (Harikedua 2010), the first indicator of appearance that can be directly observed by consumers in a product. Color can affect the interest in buying or consuming a product for consumers. Nurwin et al (2019) explained that the first factor that panelists consider when choosing a product is its appearance. Although it does not directly affect the sensory level, it has a strong impact on consumer acceptance. The KruskallWallis test on the hedonic value of appearance showed that there was no significant effect on the addition of collagen at concentrations of 0, 1, 2, and 3% on the appearance of yujacha collagen drink. Thus, Ho (increasing concentration has no effect) on the appearance of yujacha collagen drink) was accepted and no further testing was carried out.
The highest result for odor was obtained in control, with a value of 4.07, and the lowest at a collagen concentration of 3%, with a value of 3.13. The odor of yujacha collagen drinks with the addition of collagen 1 and 2% obtained average results of 3.60 and 3.43, respectively. Wijaya et al (2021), revealed that collagen extract slightly smells the fish because it is extracted from aquatic animals. Odor is an important parameter where odor greatly influences the consumer acceptance (Rahayu et al 2020). The Kruskall-Wallis test on the hedonic value of the odor or aroma parameter obtained an Asymp. Sig. value of less than 0.05 at a 95% confidence level. These results show that there is a real effect of the addition of collagen at concentrations of 0, 1, 2, and 3% on the odor of yujacha collagen drinks. The results of the Mann Whitney further test on the odor parameter prove that the addition of 1% collagen is significantly different from the addition of 3% collagen, but not significantly different from the addition of 2% collagen, and that the addition of 2% collagen is not significantly different from the addition of 3% collagen.
The highest flavour value was obtained in control, with a value of 4.03, and the lowest with a concentration of 3%, with a value of 3.43. The taste of yujacha drinks with the addition of collagen 1 and 2% obtained average results of 3.53 and 3.50, respectively. The Kruskall-Wallis test on the hedonic value of the taste parameter obtained an Asymp. Sig. value of less than 0.05 at a 95% confidence level. So, from these results there is a real effect on the addition of collagen at concentrations of 0, 1, 2, and 3% on the taste of yujacha collagen drinks. The results of the Mann Whitney test on the taste parameters provides a real difference between control and the treatments with 1, 2, and 3% collagen, and there is no real difference between the addition of 1, 2, and 3% collagen.
The texture parameters showed the highest results when collagen was added at a concentration of 1%, with a value of 4.03, and the lowest at a concentration of 2%, with a value of 3.77. Kruskall-Wallis test on the hedonic value of texture obtained an Asymp. Sig. value greater than 0.05 at a 95% confidence level. This shows that the texture of collagen drinks yujacha is not no significantly influenced by the addition of collagen at concentrations of 1, 2, and 3%.
Conclusions. Collagen extraction from Thunnus sp. skin produces high-quality collagen with a protein content of 86.55%, low moisture content (7.02%), and ash content (0.67%) that meets SNI standards. Collagen shows a strong antioxidant activity, with a value of 151.65 pmol Fe> gi and the content of dominated by the following amino acids: glycine, proline, and arginine. Its application to citrus honey tea (yujacha) beverages improves viscosity, pH, and sensory stability, although there is a decrease in hedonic receptivity to aroma and taste, with increased collagen concentrations. These results support the use of fish collagen as an innovative ingredient for functional food products.
Conflict of interest. The authors declare that there is no conflict of interest.
References
Adrianar N., Batubara R., Julianti E., 2015 [Value of consumers preference towards to agarwood tea leaves (Aquilaria malaccensis Lamk) based on the location of leaves in the trunk]. Peronema Forestry Science Journal 4(4):12-16. [in Indonesian]
Afifah A., Suparno O., Haditjaroko L., Tarman K., 2019 Utilization of fish skin waste as a collagen wound dressing on burn injuries: a mini review. IOP Conference Series: Earth and Environmental Science 335(1):012-031.
Afifah A., Suparno O., Haditjaroko L., Tarman K., Setiyono A., Nugraha A. W., 2023 Isolation and characterization of collagen from salmon (Salmo salar) skin using acid method. Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 18(2):139-147.
Alhana, Suptijah P., Tarman K., 2015 [Extraction and characterization of collagen from Gamma Sea cucumber meat]. Indonesian Journal of Fisheries Product Processing 18(2):150-161. [in Indonesian]
Andakke J. N., Rumengan I. F. M., Nainggolan H. H. Y., Parapat L. R. M. E., Pandey E., Suptijah P., Luntungan A. H., 2020 [Molecular structure of gelatin extracted from parrot fish (Scarus sp) scales]. Coastal And Tropical Marine Journal 8(1):15-19. [in Indonesian]
Ardhani, Safithri M., Tarman K., Husnawati, Setyaningsih I., Meydia, 2019 Antioxidant activity of collagen from skin of parang-parang fish (Chirocentrus dorab) using DPPH and CUPRAC methods FAK. IOP Conference Series: Earth and Environmental Science 012032:1-9.
Bilek S. E., Bayram S. K., 2015 Fruit juice drink production containing hydrolyzed collagen. Journal of Functional Foods 3(12):562-569.
Choi J., Kim J. K., Kim J. H., Kweon D. K., Lee J. W., 2010 Degradation of hyaluronic acid powder by electron beam irradiation. Physical and sensory characteristics of pedada fruit juice beverage. Indonesian Journal of Fishery Product Processing 23(3):532541.
Dari D. W., Jumita D., 2020 [Physical and sensory characteristics of pedada fruit juice drink]. Jurnal Pengolahan Hasil Perikanan Indonesia 23(3):532-541. [in Indonesian]
Devi Н. L. № A., Suptijah P., Nurilmala M., 2017 [Effectiveness of alkali and acid on collagen quality from pangasius catfish skin]. Indonesian Journal of Fishery Product Processing 20(2):255-265. [in Indonesian]
Devita L., Lioe H. N., Nurilmala M., Suhartono M. T., 2021 The bioactivity prediction of peptides from tuna skin collagen using integrated method combining in vitro and in silico. Foods 10(11):27-39.
Dwiloka B., Rahman F. T., Mulyani S., 2022 [pH, viscosity and hedonic value of sweet orange juice with the addition of milkfish bone gelatin]. Journal of Agri-food, Nutrition and Public Health 2(2):107-113. [in Indonesian]
El Blidi O., El Omari N., Balahbib A., Ghchime R., El Menyiy N., Ibrahimi A., Kaddour K. B., Bouyahya A., Chokairi O., Barkiyou M., 2021 Extraction methods, characterization and biomedical applications of collagen: a review. Biointerface Research in Applied Chemistry 11(5):13587-13613.
Foggia M. D., Taddei P., Torreggiani A., Dettin M., Tinti A., 2011 Self-assembling peptides for biomedical applications: IR and Raman Spectroscopies for the study of secondary structure. Journal of Proteomics Research 2(3):232-272.
Harikedua S. D., 2010 [Effect of adding ginger water extract (Zingiber officianle Rosceo) and cold storage on the sensory quality of tuna (Thunnus albacares)]. Journal of Fisheries and Marine 6(1):36-40. [in Indonesian]
Hawa L. C., Komar N., Wirayanti D., 2016 [Combination of thermal and non-thermal pasteurization on citrus juice]. Journal of Tropical Agricultural and Biosystems Engineering 4(3):242-249. [in Indonesian]
Hema G. S., Shyni K., Mathew S., Ananda R., Ninan G., Lakshmanan, 2013 A simple method for isolation of fish skin collagen biochemical characterization of skin collagen extracted from albacore tuna (Thunnus alalunga), dog shark (Scoliodon sorrakowah) and rohu (Labeo rohita). Annals of Biological Research 4(1):271-278.
Huang С. Y., Kuo J. M., Wu S. J., Tsai H. T., 2016 Isolation and characterization of fish scale collagen from tilapia (Oreochromis sp.) by a novel extrusion-hydro-extraction process. Food Chemistry 190(4):997-1006.
Hursepuny J. J., Moniharapon T., Mailoa M. M., 2021 Chemical and microbiological characteristics bakasang ofinnards yellowfin tuna (Thunnus albacares). Journal of Fisheries Product Technology 1(2):86-99.
Ibrahim A., Soliman M., Kotb S., Ali M. M., 2020 Evaluation of fish skin as a biological dressing for metacarpal wounds in donkeys. BMC Veterinary Research 16(472):1-10.
Jacoeb A. M., Nurjanah, Lingga, 2012 [Characteristics of protein and amino acids of crab meat (Portunus pelagicus) due to steaming]. Indonesian Journal of Fisheries Product Processing 15(2):156-163. [in Indonesian]
Kolanus J. Р. M., Hadinoto S., Idrus S., 2019 [The characterization of collagen acid soluble from yellowfin tuna (Thunnus albacares) fish skin by using hydroectraction method]. Journal of Industrial Technology Research 13(1):99-110. [in Indonesian]
Kong J., Yu S., 2007 Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica 39(8):549-559.
Kong S., Lv L., Guo J., Yang X., Liao M., Zhao T., Sun H., Zhang S., Li W., 2023 Preparation of cod skin collagen peptides/chitosan-based temperature-sensitive gel and its antiphotoaging effect in skin. Drug Design, Development and Therapy 17(11):419-437.
Kristoffersen K. A., Mage I., Wubshet 5. G., Bócker U., Dankel К. R., Lislelid A., Renningen M. A., Afseth N. K., 2023 FTIR-based prediction of collagen content in hydrolyzed protein samples. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 301:1-8.
Kumalasari R., Ekafitri R., Desnilasari R., 2015 [Effect of stabilizer material and fruit pulp ratio on the quality of mixed papaya and pineapple fruit juice]. Journal of Horticulture 25(3):266-276. [in Indonesian]
Kusa S. R., Silvana A. N., Nikmawatisusanti Y., 2022 [Characteristics of yellowfin tuna (Thunnus sp.) skin collagen at different hydro-extraction times and its potential in the form of nanocollagen preparations]. Fishery Product Technology Media 10(2):107-116. [in Indonesian]
Li Z., Wang B., Chi C., Zhang Q., Gong Y., Tang J., Luo H., Ding G., 2013 Isolation and characterization of acid soluble collagens and pepsin soluble collagens from the skin and bone of spain mackerel (Scomberomorous niphonius). Food Hydrocolloids 31:103-113.
Maharani S. A., 2018 [Characteristics of jelly drink with fortification of collagen of tuna fish skin (Thunnus albacares)]. IPB University, Bogor, 85 p. [in Indonesian]
Muyonga J. H., Cole C. G. B., Duodu K. G., 2004a Fourier Transform Infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chemical 86(3):325-332.
Nagarajan M., Benjakul S., Prodpran T., Songtipya P., Kishimura H., 2012 Characteristics and functional properties of gelatin from splendid squid (Loligo formosana) skin as affected by extraction temperatures. Food Hydrocolloids 29:389-397.
Nurjanah N., Abdullah A., Nufus C., 2018 [Characteristics of Ulva lactuca salt preparation from Sekotong Waters, West Nusa Tenggara for hypertension patients]. Indonesian Journal of Fisheries Product Processing 21(1):109. [in Indonesian]
Nurjanah, Baharuddin T. I, Nurhayati T., 2021 [Extraction of yellowfin tuna (Thunnus sp.) skin collagen using pepsin and papain enzymes]. Indonesian Journal of Fisheries Product Processing 24(2):174-187. [in Indonesian]
Nurwin A. F., Dewi E. N., Romadhon, 2019 [The effect of adding carrageenan flour on the characteristics of blood clam meatballs (Anadara granosa)]. Journal of Fisheries Science and Technology 1(2):39-46. [in Indonesian]
Permata D. A., Sayuti K., 2016 [Making instant powdered drinks from various parts of the Phyllanthus niruri plant]. Andalas Journal of Agricultural Technology 20(1):44-49. [in Indonesian]
Prestes R. C., Graboski A., Roman S. S., Kempka A. P., Toniazzo G., Demiate I. M., Di Luccio M., 2013 Effects of the addition of collagen and degree of comminution in the quality of chicken ham, Journal of Applied Poultry Research 22(4):885-903.
Rahantan M., Lalopua V. M. N., Savitri I. K. E., 2024 [Quality characteristic of collagen extracted from tuna loin production waste]. Biopendix: Journal of Biology, Education and Applied 10:234-243. [in Indonesian]
Rahayu W. E., Sa'diyah 5. H., Romalasari A., 2020 [Effect of application time and concentration of red guava juice (Psidium guajava L.) addition on goat milk kefir]. Agromix 11(1):1-8. [in Indonesian]
Rakhmawati R., Yunianta Y., 2015 [Effect of water fruit proportion and heating time on antioxidant activity of kedondong fruit juice (Spondias dulcis)]. Journal of Food and Agroindustry 3(4):1682-1693. [in Indonesian]
Sembiring T. E. S., Reo A. R., Onibala H., Montolalu К. I., Taher N., Mentang F., Damongilala L. J., 2020 [Extraction of tuna (7hunnus sp.) bone collagen with hydrochloric acid]. Fisheries Product Technology Media 8(3):107-110. [in Indonesian]
Shakila G., Periandy S., Ramalingam S., 2012 Vibrational spectroscopic investigation (FTIR and FT-Raman) on 1,2-dibromobenzene by HF and hybrid (LSDA and B3LYP) calculations. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 86:449-455,
Shon J., Ji-Hyun E., Hwang S. J., Jong Bang E., 2011 Effect of processing conditions on functional properties of collagen powder from skate (Raja kenojei) skins. The Journal of Food Science Biotechnology 20(1):99-106.
Suptijah P., Indriani D., Wardoyo S. E., 2018 [Isolation and characterization of collagen from skin of catfish (Pangasius sp.)]. Journal of Natural Science 8(1):8-23. [in Indonesian]
Tumilaar S. G., Hardianto A., Dohi H., Kurnia D., 2024 A comprehensive review of free radicals, oxidative stress, and antioxidants: Overview, clinical applications, global perspectives, future directions, and mechanisms of antioxidant activity of flavonoid compounds. Journal of Chemistry 594386, 21 p.
Utami R., Trilaksani W., Hardiningtyas S. D., 2024 [Characteristics of papain soluble collagen from swim bladder of manyung fish with variations of alkali pretreatment and extractant ratio]. Journal of Fishery Product Processing 27(3):223-241. [in Indonesian]
Wahyudi H., Adlim, Nasir M., 2022 Antioxidant activity test of extract fruit (Annona squamosa L.) young and mature with FRAP method (Ferric Reducing Antioxidant Power). Al-Kimia 10(1):42-52.
Wang W., Li Z., Liu J., Wang Y., Liu S., Sun M., 2013 Comparison between thermal hydrolysis and enzymatic proteolysis processes for the preparation of tilapia skin collagen hydrolysate. Journal of Food Science 31(1):1-4.
Widyantari A., 2020 [Functional beverage formulation against antioxidant activity]. Health Widya 2(1):22-29. [in Indonesian]
Wijaya A., Junianto, Subiyanto, Pratama R. A., 2021 [The effect of collagen concentration from tilapia fish bones on the quality of skin cream]. Terubuk Fisheries Periodical 49(3):1131-1141. [in Indonesian]
Yanti F., Dharmayanti N., Suryanti, 2022 [Antioxidant activity of collagen from catfish skin (Pangasius sp.) with crude bromelain enzyme from pineapple skin (Ananas comosus L.)]. Indonesian Journal of Fishery Product Processing 25(1):1-9. [in Indonesian]
*·· AOAC, Association of Official Analytical Chemists, 2005 Official method of analysis of The Association of Official Analytical Chemists. The Association of Official Analytical Chemists Inc., 15th ed., Washington D.C., USA, 1094 p.
*·· FAO, 2012 The state of food and agriculture. FAO, Rome, Italy, 165 p.
*·· Indonesian National Standard, SNI, 2006 [SNI 01-2354.4-2006 Chemical test methods - Part 4: Determination of protein content by the total nitrogen method in fishery products]. National Standardization Agency, Jakarta, Indonesia, 10 p. [in Indonesian]
*·· Indonesian National Standard, SNI, 2010 [SNI 2354.1:2010 Chemical test methods- Part 1: Determination of ash and acid-insoluble ash content in fishery products]. National Standardization Agency, Jakarta, Indonesia, 9 p. [in Indonesian]
*·· Indonesian National Standard, SNI 2015 [SNI 2354.2:2015 Chemical test methods - Part 2: Testing water content in fishery products]. National Standardization Agency, Jakarta, Indonesia, 8 p. [in Indonesian]
*·· Indonesian National Standard, SNI 2017 [SNI 2354-3:2017 Chemical test methods - Part 3: Determination of total fat content in fishery products]. National Standardization Agency, Jakarta, Indonesia, 15 p. [in Indonesian]
*·· Indonesian National Standard, SNI 2020 [SNI 8709:2020 Karaage]. National Standardization Agency, Jakarta, Indonesia, 23 p. [in Indonesian]
Copyright Bioflux SRL 2025