Characterization of Low-Molecular-Weight Collagen from Korean Native Chicken Feet Hydrolyzed Using Alcalase
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The aims of this study were to optimize the preparation of low-molecular-weight collagen using a proteolytic enzyme (alcalase) derived from the feet of Korean native chickens, and to characterize the process of collagen hydrolysis. Foreign bodies from chicken feet were removed using ultrasonication at 28 kHz with 1.36 kW for more than 25 min. The hydrolytic pattern and molecular weight distribution of enzyme-treated collagen from chicken feet were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high-performance liquid chromatography, respectively. Ideally, chicken feet should be treated at 100°C for 8 h to obtain a high collagen content using hot water extraction. The collagen content of the chicken foot extract was 13.9 g/100 g, and the proportion of low-molecular-weight collagen increased with increasing proteolytic enzyme concentration and reaction time. When treated with 1% alcalase, the average molecular weight of collagen decreased rapidly to 4,929 Da within 5 h and thereafter decreased at a slower rate, reaching 4,916 Da after 7 h. Size exclusion chromatography revealed that low-molecular-weight collagen peptides of approximately 1,000–5,000 Da were obtained after hydrolysis with 1% alcalase for 1 h.
Abstract
The aims of this study were to optimize the preparation of low-molecular-weight collagen using a proteolytic enzyme (alcalase) derived from the feet of Korean native chickens, and to characterize the process of collagen hydrolysis. Foreign bodies from chicken feet were removed using ultrasonication at 28 kHz with 1.36 kW for more than 25 min. The hydrolytic pattern and molecular weight distribution of enzyme-treated collagen from chicken feet were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high-performance liquid chromatography, respectively. Ideally, chicken feet should be treated at 100°C for 8 h to obtain a high collagen content using hot water extraction. The collagen content of the chicken foot extract was 13.9 g/100 g, and the proportion of low-molecular-weight collagen increased with increasing proteolytic enzyme concentration and reaction time. When treated with 1% alcalase, the average molecular weight of collagen decreased rapidly to 4,929 Da within 5 h and thereafter decreased at a slower rate, reaching 4,916 Da after 7 h. Size exclusion chromatography revealed that low-molecular-weight collagen peptides of approximately 1,000–5,000 Da were obtained after hydrolysis with 1% alcalase for 1 h.
참고문헌 (26)
- Acemoglu D, "Disease and development: the effect of life expectancy on economic growth", J. Poli. Econ, 115, pp.925~985 (2007)
- Ministry of Food and Drug Safety, "Food and Drug Industry Trend Statistics", ~ (2021)
- Khiari Z, "Low molecular weight bioactive peptides derived from the enzymatic hydrolysis of collagen after isoelectric solubilization", precipitation process of turkey by-products, 2014, pp.93, 2347~2362
- Sionkowska A, "The review of versatile application of collagen", Poly. Adv. Technol, 28, pp.4~9 (2017)
- Zhao X, "Collagen peptides and the related synthetic peptides: a review on improving skin health", J. Funct. Foods, 86, pp.104680~ (2021)
- Wang H, "A review of the effects of collagen treatment in clinical studies", Polymers, 13, pp.3868~ (2021)
- Lugo JP, "Undenatured type II collagen (UC-II®) for joint support: a randomized, double-blind, placebo-controlled study in healthy volunteers", J. Int. Soc. Sports Nutr, 10, pp.48~ (2013)
- Asserin J, "The effect of oral collagen peptide supplementation on skin moisture and the dermal collagen network: evidence from an ex vivo model and randomized, placebo-controlled clinical trials", J. Cosmet. Dermatol, 14, pp.291~301 (2015)
- Li P, "Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth", Amino Acids, 50, pp.29~38 (2018)
- Silva CML, "Fast and sensitive collagen quantification by alkaline hydrolysis", hydroxyproline assay, 2015, pp.173, 619~623
- Koopman R, "Ingestion of a protein hydrolysate is accompanied by an accelerated in vivo digestion and absorption rate when compared with its intact protein", Am. J. Clin. Nut, 90, pp.106~115 (2009)
- Huang CY, "Evaluation of iron-binding activity of collagen peptides prepared from the scales of four cultivated fishes in Taiwan", J. Food Drug Anal, 23, pp.671~678 (2015)
- Harris M, "Developments for collagen hydrolysate in biological, biochemical, and biomedical domains: a comprehensive review", Materials, 14, pp.2806~ (2021)
- Santana JCC, "Valorization of chicken feet by-product of the poultry industry: high qualities of gelatin and biofilm from extraction of collagen", Polymers, 12, pp.529~ (2020)
- Dhakal D, "Optimization of collagen extraction from chicken feet by papain hydrolysis and synthesis of chicken feet collagen based biopolymeric fibres", Food Biosci, 23, pp.23~30 (2018)
- Delgado LM, "Acetic acid and pepsin result in high yield, high purity and low macrophage response collagen for biomedical applications", Biomed. Mater, 12, pp.065009~ (2017)
- Jayathilakan K, "Utilization of byproducts and waste materials from meat, poultry and fish processing industries: a review", J. Food Sci. Technol, 49, pp.278~293 (2012)
- AOAC, "Method 928.08. Official Methods of Analysis of AOAC Intl., 20th Ed", Association of Official Analytical Chemists, ~ (2016)
- Kolar K, "Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat products: NMKL collaborative study", J. Assoc. Off. Anal. Chem, 73, pp.54~57 (1990)
- Edwards CA, "Modified assay for determination of hydroxyproline in a tissue hydrolyzate", Clin. Chim. Acta, 104, pp.161~167 (1980)
- Laemmli UK, "Cleavage of structural protein during the assembly of the head of bacteriophage T4", Nature, 227, pp.680~685 (1970)
- Widyasari R, "Extraction and characterization of gelatin from chicken feet by acid and ultrasound assisted extraction", Food Appl. Biosci. J, 2, pp.85~97 (2014)
- Potti RB, "Extraction and characterization of collagen from broiler chicken feet (Gallus gallus domesticus) -biomolecules from poultry waste", J. Pure Appl. Microbiol, 11, pp.315~322 (2017)
- Hong H, "Preparation of low-molecular-weight, collagen hydrolysates (peptides): current progress, challenges, and future perspectives", Food Chem, 301, pp.125222~ (2019)
- Zhang Y, "Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACEinhibitory peptides", Food Chem, 141, pp.2343~2354 (2013)
- Antosova Z, "Therapeutic application of peptides and proteins: parenteral forever?", Trends Biotechnol, 27, pp.628~635 (2009)