Effect of Different Papain Concentrations on the Properties of Chicken Skin Protein Hydrolysates

Chicken skin is a source of animal protein hydrolysate, which has a potential as an antioxidant. This study aimed to determine the effect of different concentrations of the enzyme papain on the degree of hydrolysis, antioxidant capacity, percentage of reducing power (%RP) and amino acid composition of chicken skin protein hydrolysate. Hydrolysis was carried out using papain with various concentrations (3%, 4% and 5%, w/w protein substrate) at pH 7 and 50℃ for 6 h. The degree of hydrolysis was determined by spectrophotometry. Antioxidant capacity and %RP was determined by ferric reducing antioxidant power method and expressed in milligram of ascorbic acid equivalent per gram of sample, and amino acid composition were determined using high-performance liquid chromatography. The results showed that variations in papain concentration had a significant effect (P<0.05) on the degree of hydrolysis, antioxidant capacity and %RP of chicken skin hydrolysate. The papain concentration of 4% resulted in the optimum protein hydrolysate with a degree of hydrolysis of 61.68%±0.64%, an antioxidant capacity of 8.72±0.30 mg AA/g sample and a %RP of 54.12%±1.78%. The protein hydrolysates of the treated chicken skin showed a high content of amino acids, namely, glycine, glutamate, proline, arginine and aspartate.

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Muscle Protein Hydrolysates and Amino Acid Composition in Fish

Marine Drugs ◽

10.3390/md19070377 ◽

2021 ◽

Vol 19 (7) ◽

pp. 377

Author(s):

Bomi Ryu ◽

Kyung-Hoon Shin ◽

Se-Kwon Kim

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Muscle Protein ◽

Fish Muscle ◽

Amino Acid Profile ◽

Industrial Applications ◽

Protein Hydrolysates ◽

Added Value ◽

Degree Of Hydrolysis

Fish muscle, which accounts for 15%–25% of the total protein in fish, is a desirable protein source. Their hydrolysate is in high demand nutritionally as a functional food and thus has high potential added value. The hydrolysate contains physiologically active amino acids and various essential nutrients, the contents of which depend on the source of protein, protease, hydrolysis method, hydrolysis conditions, and degree of hydrolysis. Therefore, it can be utilized for various industrial applications including use in nutraceuticals and pharmaceuticals to help improve the health of humans. This review discusses muscle protein hydrolysates generated from the muscles of various fish species, as well as their amino acid composition, and highlights their functional properties and bioactivity. In addition, the role of the amino acid profile in regulating the biological and physiological activities, nutrition, and bitter taste of hydrolysates is discussed.

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PRODUKSI HIDROLISAT PROTEIN ANTIOKSIDAN MELALUI HIDROLISIS ENZIMATIK PROTEIN KULIT AYAM BROILER DENGAN ENZIM PAPAIN

Jurnal Kimia ◽

10.24843/jchem.2020.v14.i02.p16 ◽

2020 ◽

pp. 206

Author(s):

N. M. Puspawati ◽

P. P. Dewi ◽

N. W. Bogoriani ◽

N. K. Ariati

Keyword(s):

Antioxidant Activity ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Degree Of Hydrolysis ◽

Dpph Radical ◽

Hydrolysis Time ◽

Protein Hydrolyzate ◽

Chicken Skin ◽

Hydrolysis Of

Penelitian ini bertujuan untuk menentukan aktivitas antioksidan hidrolisat protein yang dihasilkan dari proses hidrolisis enzimatik protein kulit ayam dengan menggunakan variasi konsentrasi enzim papain. Proses hidrolisis dilakukan dengan variasi konsentrasi enzim 1, 3,dan 5% (b/b protein), pada pH 7, suhu 50oC dan waktu hidrolisis 24 jam. Parameter yang diukur meliputi derajat hidrolisis, persen peredaman radikal DPPH (diphenylpicryl hidrazyl), dan komposisi asam amino hidrolisat protein yang paling aktif antioksidan. Hasil penelitian menunjukkan penggunaan konsentrasi enzim yang berbeda menghasikan hidrolisat protein dengan derajat hidrolisis dan persen peredaman DPPH yang berbeda. Penggunaan konsentrasi enzim papain 1, 3, dan 5% menghasilkan hidrolisat protein dengan derajat hidrolisis berturut-turut sebesar 9,3±1,8, 18,09±5,6, dan 23,15±6.33%, dan persentase hambatan radikal DPPH pada konsentrasi uji 100 ppm berturut-turut sebesar 16,75±0,07, 58,35±0,00, dan 52,99±0,07%. Hidrolisat protein yang diperoleh menggunakan enzim papain 3% (b/b protein) menunjukkan persen peredaman tertinggi dengan nilai IC50 92,98 ppm, memiliki komposisi asam amino tertiggi asam glutamat dan terendah valine. Kata kunci: antioksidan, enzim papain, hidrolisat protein, kulit ayam This study aimed to determine the antioxidant activity of protein hydrolyzate produced from the enzymatic hydrolysis of chicken skin protein by using variations of the enzyme papain concentration. The hydrolysis process was carried out with variations in the concentration of the enzymes 1, 3, and 5% (w/w protein base), at pH 7, temperature 50oC, and hydrolysis time 24 hours. The parameters measured including degree of hydrolysis, percentage of inhibition of DPPH radical (diphenylpicryl hydrazyl) and amino acid composition of the protein hydrolyzate with the highest antioxidant activity. The results showed that the use of different enzyme concentrations resulted in protein hydrolyzate with different degrees of hydrolysis and percentage of inhibition of DPPH. The use of papain enzymes 1, 3, and 5% produced protein hydrolyzate with the degree of hydrolysis of 9.3 ± 1.8, 18.09 ± 5.6, and 23.15 ± 6.33%, and the percentage of inhibition of DPPH radical at a concentration of 100 ppm 16.75 ± 0.07, 58.35 ± 0.00, and 52.99 ± 0.07% respectively. Protein hydrolyzate obtained using the enzyme papain 3% (w/w protein) exhibited the highest percentage of inhibition of DPPH with an IC50 value of 92.98 ppm, having the highest amino acid composition of glutamic acid and the lowest valine. Keywords: antioxidant, enzyme papain, protein hydrolyzate, chicken skin

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Potential Use of Tuna (Thunnus albacares) by-product: Production of Antioxidant Peptides and Recovery of Unsaturated Fatty Acids from Tuna Head

International Journal of Food Engineering ◽

10.1515/ijfe-2015-0365 ◽

2017 ◽

Vol 13 (7) ◽

Cited By ~ 3

Author(s):

Dayse Oliveira ◽

Daniela Bernardi ◽

Fernanda Drummond ◽

Fabiana Dieterich ◽

Wilson Boscolo ◽

...

Keyword(s):

Fatty Acids ◽

Antioxidant Capacity ◽

Unsaturated Fatty Acids ◽

Protein Hydrolysate ◽

Trolox Equivalent Antioxidant Capacity ◽

Total Amino Acid ◽

Degree Of Hydrolysis ◽

Antioxidant Peptides ◽

Antioxidant Power ◽

By Products

AbstractTuna by-products were subjected to enzymatic hydrolysis with Alcalase (enzyme to substrate ratio 1 : 200 w/w; 60 °C; pH 6.5, 120 min) rendering a tuna protein hydrolysate (TPH) with 9.24 % degree of hydrolysis (DH). The antioxidant capacity of TPH determined by the methods of ferric reducing antioxidant power (FRAP) and Trolox equivalent antioxidant capacity (TEAC) were similar and 10 times lower than the result obtained by oxygen radical absorbance capacity (ORAC). The total amino acid profile indicated that 42.15 % are composed of hydrophobic amino acids and 7.7 % of aromatics, with leucine being found in the highest quantity (17.85 %). The fatty acid profile of the oil recovered by centrifugation of the TPH – as determined by a gas chromatograph – was characterized by a high percentage of polyunsaturated fatty acids (PUFAs) (39.06 %), mainly represented by the fatty acids ω3, docosahexaenoic acid (27.15 %) and eicosapentaenoic acid (6.05 %). The simultaneous recovery of unsaturated fatty acids and antioxidant peptides can add value to tuna by-products, assisting in the efficient management of fishing industry waste.

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Homology between a histidine-rich protein from Plasmodium lophurae and a protein associated with the knob-like protrusions on membranes of erythrocytes infected with Plasmodium falciparum.

Journal of Experimental Medicine ◽

10.1084/jem.151.6.1534 ◽

1980 ◽

Vol 151 (6) ◽

pp. 1534-1538 ◽

Cited By ~ 38

Author(s):

A Kilejian

Keyword(s):

Amino Acids ◽

Plasmodium Falciparum ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Immunoelectron Microscopy ◽

Protein Hydrolysate ◽

Cross Reactivity ◽

Plasmodium Lophurae

The incorporation of several radioactive amino acids into the knob protein of Plasmodium falciparum was compared. Histidine showed better incorporation than proline. A protein hydrolysate, which had all major amino acids except histidine and methionine, showed relatively poor incorporation as compared with proline, and no labeling could be detected with methionine or leucine. These results strongly suggest that the amino acid composition of the knob protein has the same peculiarities as that of a histidine-rich protein characterized from P. lophurae. Immunoelectron microscopy suggested possible immunological cross-reactivity between these two proteins.

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