Characterization of collagen and its hydrolysate from yellowfin tuna Thunnus albacares skin and their potencies as antioxidant and antiglycation agents

Nurilmala, Mala; Pertiwi, Rizsa Mustika; Nurhayati, ‪Tati; Fauzi, Shita; Batubara, Irmanida; Ochiai, Yoshihiro

doi:10.1007/s12562-019-01303-5

Cited by 34 publications

(34 citation statements)

References 32 publications

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“…Collagen was extracted according to the method in our previous report [6]. Pretreatment of tuna skin consisted of two steps, the removal of non-collagenous protein followed by the removal of fat.…”

Section: Preparation Of Collagenmentioning

confidence: 99%

“…Tuna bones and skins are generally used only to feed cattle with reduced selling price. For value addition, the skin waste from industrial tuna loins as well as fillets can be utilized as the materials for collagen and gelatin [5][6][7]. However, a large amount of tuna skin has remained underutilized, despite the fact that it can be an excellent source of collagen and gelatin, provided that they are demonstrated to be of high quality.…”

Section: Introductionmentioning

confidence: 99%

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Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

et al. 2020

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Skin waste from tuna processing needs to be utilized, such as extraction of its collagen and gelatin. Their functional properties can be improved by enzymatic hydrolysis for conversion to peptides. Thus, the research objectives were to examine the characteristics and antioxidant activity of collagen, gelatin, and the derived peptide from yellowfin tuna skin. Collagen was extracted using 0.75 M acetic acid at 4 °C, while gelatin was prepared using 0.25% citric acid and extracted at 65 °C. Hydrolysis was carried out with 2% Alcalase, followed by fractionation with a molecular weight cut off sieve for both collagen and gelatin. Collagen yield was 22.6% with pH value of 6.63 and whiteness of 96.7%. Gelatin yield was 20.0% with pH value of 4.94 and whiteness of 51.0%. Hydrolysis for three hours resulted in 52.7% and 45.2% degree of hydrolysis for collagen and gelatin, respectively. The molecular weights of collagen peptides ranged from 2.94 to 11.93 kDa, while those of gelatin peptides ranged from 3.54 to 16,620 kDa. Antioxidant activities of these peptides were higher than those before hydrolysis. The high antioxidant activity (IC50) of collagen peptides were found in <3, 3–10, and 10–30 kDa fractions as well as in the gelatin peptides.

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Section: Preparation Of Collagenmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

et al. 2020

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“…Fig 5. Wu et al (2014) 39 ; was purified trypsin inhibitor from Yellowfin Tuna (Thunnus Albacores) , done by column chromatography with Sephacry S-200, Sephadex G-50, and DEAE-cellulose and found to have an apparent molecular weight of 7 × 104 Da. Mala Nurilmala et al, (2019) 40 reported that the collagen obtained from yellowfin tuna Thunnus albacares skin was further hydrolyzed with alcalase, and the peptides fractionated by gel filtration chromatography. The highest solubility for both skin and muscle type 1 collagen obtained from Uroteuthis duvauceli were found to be at pH 3 and pH 4 respectively.…”

Section: Resultsmentioning

confidence: 99%

Extraction and Purification of Collagen from Marine Squid Uroteuthis Duvauceli

George

Manjusha²

2022

Int J Life Sci Pharm Res

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Collagen is a protein, which plays a significant role in the development of tissues and organs. These are used for cosmetic surgery and as wound healing aids in burn patients, remaking of bone and a wide assortment of dental, orthopedic and surgical purposes. These days' collagen is isolated from calf, porcine tissue and so forth. But it can cause the onset of diseases such as, for example, Bovine spongiform encephalopathy (BSE), Transmissible spongiform encephalopathy (TSE), Foot-and-mouth illness (FMD), and so forth and furthermore cultural and social concerns. As another option, collagen can be separated from marine squid. The aim of the present work is to isolate and partially characterize the collagen from the marine squid, Uroteuthis duvauceli. The confined collagen was evaluated by utilizing Bradford test and partially purified by using gel filtration on a Sepharose 4B column. These filtered collagens were affirmed by SDS PAGE. These days industrially accessible collagen in the market are costly and are not affordable to the common people. The present data on collagens from the marine squid, could help the future endeavors to unwind the therapeutically significant, more secure collagens from marine squid for their utilization in the biomedical field.

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“…Perlakuan konsentrasi enzim 5.000 U/ mg tidak berbeda nyata dengan konsentrasi enzim 10.000 U/mg tetapi berbeda nyata dengan perlakuan konsentrasi 15.000 U/ mg dan 20.000 U/mg. Hasil ini berbeda dengan penelitian Nurilmala et al (2019) yang menjelaskan bahwa kelarutan kolagen kulit tuna yang diekstraksi dengan papain konsentrasi 3.000 U/mg, 5.000 U/mg dan 7.000 U/mg tidak memberikan efek yang signifikan terhadap kelarutan kolagen. Penambahan konsentrasi enzim papain yang lebih tinggi diduga menyebabkan enzim papain menjadi jenuh terhadap substrat sehingga dengan peningkatan konsentrasi enzim menunjukkan hasil yang tidak berpengaruh nyata.…”

Section: Ekstrak Kolagen Larut Enzim Papain Gelembung Renang Ikan Patinunclassified

Profiling of Catfish Swim Bladder Collagen (Pangasius sp.) Through Enzymatic Proses

Simamora¹,

Trilaksani²,

Uju

2019

Jurnal PHPI

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Swim bladder is a marine byproduct and a potential source of collagen needed by food, cosmetical, biomedical and pharmaceutical industry. This study evaluated the effectiveness of alkaline pretreatment and papain enzyme on the characteristics of collagen from the catfish swim bladders. TThree concentrations of alkaline (0.05; 0.1 and 0.15 M) with were used to pretreat the swim bladders for 2; 4; 6; 8; 10 and 12 hours. The collagen was also treated by papain enzyme with concentrations of 0; 5,000; 10,000; 15,000 and 20,000 U/mg for 24 and 48 hours. The result showed that pretreatment using NaOH 0.05 M for 6 hours effectively reduced the noncollagen protein (p<0.05). Meanwhile, the treatment using papain enzyme with concentration of 5.000 U/mg for 48 hours improved the collagen solubility. The FTIR of collagen showed the existence of a triple helix structure. Meanwhile, the thermal analysis showed collagen gelation transition temperature (Tg) was at 88oC.

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Characterization of collagen and its hydrolysate from yellowfin tuna Thunnus albacares skin and their potencies as antioxidant and antiglycation agents

Cited by 34 publications

References 32 publications

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

Extraction and Purification of Collagen from Marine Squid Uroteuthis Duvauceli

Profiling of Catfish Swim Bladder Collagen (Pangasius sp.) Through Enzymatic Proses

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