Hydrolyzed Collagen-Sources and Applications

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2019 Nov 10

PMID 31703345

Citations 136

Authors

Arely Leon-Lopez

Alejandro Morales-Penaloza

Victor Manuel Martinez-Juarez

Apolonio Vargas-Torres

Dimitrios I Zeugolis

Gabriel Aguirre-Alvarez

Affiliations

Soon will be listed here.

Abstract

Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3-6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.

Citing Articles

Unlocking the Potential of Marine Sidestreams in the Blue Economy: Lessons Learned from the EcoeFISHent Project on Fish Collagen.

Dondero L, De Negri Atanasio G, Tardanico F, Lertora E, Boggia R, Capra V Mar Biotechnol (NY). 2025; 27(2):63.

PMID: 40080223 PMC: 11906597. DOI: 10.1007/s10126-025-10438-9.

Bioprinting-By-Design of Hydrogel-Based Biomaterials for In Situ Skin Tissue Engineering.

Douglas A, Chen Y, Elloso M, Levschuk A, Jeschke M Gels. 2025; 11(2).

PMID: 39996653 PMC: 11854875. DOI: 10.3390/gels11020110.

Can good sleep quality enhance the benefits of oral collagen supplementation in the prevention of skin aging? A brief report.

Xerfan E, Souza M, Facina A, Tufik S, Andersen M Arch Dermatol Res. 2025; 317(1):340.

PMID: 39912934 DOI: 10.1007/s00403-025-03860-5.

Nutritional Interventions to Attenuate Quadriceps Muscle Deficits following Anterior Cruciate Ligament Injury and Reconstruction.

Smith M, Hoffman N, Jose A, Burke L, Opar D Sports Med. 2025; .

PMID: 39853659 DOI: 10.1007/s40279-025-02174-w.

How Significant Are Marine Invertebrate Collagens? Exploring Trends in Research and Innovation.

Almeida M, Silva T, Solstad R, Lillebo A, Calado R, Vieira H Mar Drugs. 2025; 23(1).

PMID: 39852504 PMC: 11766948. DOI: 10.3390/md23010002.

References

Pataridis S, Eckhardt A, Mikulikova K, Sedlakova P, Miksik I . Identification of collagen types in tissues using HPLC-MS/MS. J Sep Sci. 2008; 31(20):3483-8. DOI: 10.1002/jssc.200800351. View

Hema G, Joshy C, Shyni K, Chatterjee N, Ninan G, Mathew S . Optimization of process parameters for the production of collagen peptides from fish skin ( using response surface methodology and its characterization. J Food Sci Technol. 2017; 54(2):488-496. PMC: 5306043. DOI: 10.1007/s13197-017-2490-2. View

Jhawar N, Wang J, Saedi N . Oral collagen supplementation for skin aging: A fad or the future?. J Cosmet Dermatol. 2019; 19(4):910-912. DOI: 10.1111/jocd.13096. View

Bolke L, Schlippe G, Gerss J, Voss W . A Collagen Supplement Improves Skin Hydration, Elasticity, Roughness, and Density: Results of a Randomized, Placebo-Controlled, Blind Study. Nutrients. 2019; 11(10). PMC: 6835901. DOI: 10.3390/nu11102494. View

Lecchi P, Olson M, Brancia F . The role of esterification on detection of protonated and deprotonated peptide ions in matrix assisted laser desorption/ionization (MALDI) mass spectrometry (MS). J Am Soc Mass Spectrom. 2005; 16(8):1269-74. DOI: 10.1016/j.jasms.2005.03.019. View

Liu D, Nikoo M, Boran G, Zhou P, Regenstein J . Collagen and gelatin. Annu Rev Food Sci Technol. 2015; 6:527-57. DOI: 10.1146/annurev-food-031414-111800. View

Zhao Y, Wang Z, Zhang J, Su T . Extraction and characterization of collagen hydrolysates from the skin of . 3 Biotech. 2018; 8(3):181. PMC: 5851943. DOI: 10.1007/s13205-018-1198-y. View

Ramadass S, Nazir L, Thangam R, Perumal R, Manjubala I, Madhan B . Type I collagen peptides and nitric oxide releasing electrospun silk fibroin scaffold: A multifunctional approach for the treatment of ischemic chronic wounds. Colloids Surf B Biointerfaces. 2018; 175:636-643. DOI: 10.1016/j.colsurfb.2018.12.025. View

Bradley R . Bovine spongiform encephalopathy (BSE): the current situation and research. Eur J Epidemiol. 1991; 7(5):532-44. DOI: 10.1007/BF00143136. View

10.

Jo Y, Kim J, Jung K, Min S, Chun J . Effect of Sub- and Super-critical Water Treatment on Physicochemical Properties of Porcine Skin. Korean J Food Sci Anim Resour. 2016; 35(1):35-40. PMC: 4682499. DOI: 10.5851/kosfa.2015.35.1.35. View

11.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

12.

Leon-Lopez A, Fuentes-Jimenez L, Hernandez-Fuentes A, Campos-Montiel R, Aguirre-Alvarez G . Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity. Int J Mol Sci. 2019; 20(16). PMC: 6719941. DOI: 10.3390/ijms20163931. View

13.

Sontakke S, Jung J, Piao Z, Chung H . Orally Available Collagen Tripeptide: Enzymatic Stability, Intestinal Permeability, and Absorption of Gly-Pro-Hyp and Pro-Hyp. J Agric Food Chem. 2016; 64(38):7127-33. DOI: 10.1021/acs.jafc.6b02955. View

14.

Zou Y, Wang L, Cai P, Li P, Zhang M, Sun Z . Effect of ultrasound assisted extraction on the physicochemical and functional properties of collagen from soft-shelled turtle calipash. Int J Biol Macromol. 2017; 105(Pt 3):1602-1610. DOI: 10.1016/j.ijbiomac.2017.03.011. View

15.

Bella J, Hulmes D . Fibrillar Collagens. Subcell Biochem. 2017; 82:457-490. DOI: 10.1007/978-3-319-49674-0_14. View

16.

Gordon M, Hahn R . Collagens. Cell Tissue Res. 2009; 339(1):247-57. PMC: 2997103. DOI: 10.1007/s00441-009-0844-4. View

17.

Ramshaw J . Biomedical applications of collagens. J Biomed Mater Res B Appl Biomater. 2015; 104(4):665-75. DOI: 10.1002/jbm.b.33541. View

18.

Paschou A, Katsikini M, Christofilos D, Arvanitidis J, Ves S . High pressure Raman study of type-I collagen. FEBS J. 2018; 285(14):2641-2653. DOI: 10.1111/febs.14506. View

19.

Elavarasan K, Shamasundar B, Badii F, Howell N . Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala). Food Chem. 2016; 206:210-6. DOI: 10.1016/j.foodchem.2016.03.047. View

20.

Lima C, Campos J, Lima Filho J, Converti A, da Cunha M, Porto A . Antimicrobial and radical scavenging properties of bovine collagen hydrolysates produced by Penicillium aurantiogriseum URM 4622 collagenase. J Food Sci Technol. 2015; 52(7):4459-66. PMC: 4486589. DOI: 10.1007/s13197-014-1463-y. View