Wild Caught Marine Collagen Peptides Powder
Description
PRODUCT DETAILS
- Hydrolyzed collagen
- Marine source of collagen type 1 & 3
- Meatless collagen
- Sustainably sourced deep-water ocean white fish from North America cold waters
- 18 amino acids
- Non-GMO
- Dairy & gluten-free
- Zero carbs
- Pure collagen: no additives, preservatives or sulfites
- Mix in beverages, protein shakes, and food recipes
- Manufactured in the USA in a cGMP certified facility
- Third party tested
- 50 days supply
Wild-Caught Fish Collagen
MARINE COLLAGEN 202
FEATURED INGREDIENTS
Wild Caught Hydrolyzed Fish Collagen
Types 1 & 3 collagen from white fish

Glycine
Abundant amino acid found in collagen*

Proline
Amino acid involved in proteins biosynthesis

Hydroxyproline
Amino acid involved in collagen stabilization


Our oceans are a wonderful source of life. When we designed our marine collagen, we wanted the formula to represent the idea of purity, simplicity, and calmness. A glimpse of the wonders of marine life here on earth.
Pure marine collagen peptides powder of type I & III, sustainably sourced, and easy to use
Non-GMO. Meatless. Manufactured in the USA. 3rd party tested.
Supplement Facts
Ingredients
Suggested Use
References
- Description
- Supplement Facts
- Ingredients
- Suggested Use
- References
PRODUCT DETAILS
- Hydrolyzed collagen
- Marine source of collagen type 1 & 3
- Meatless collagen
- Sustainably sourced deep-water ocean white fish from North America cold waters
- 18 amino acids
- Non-GMO
- Dairy & gluten-free
- Zero carbs
- Pure collagen: no additives, preservatives or sulfites
- Mix in beverages, protein shakes, and food recipes
- Manufactured in the USA in a cGMP certified facility
- Third party tested
- 50 days supply
Wild-Caught Fish Collagen
MARINE COLLAGEN 202
FEATURED INGREDIENTS
Wild Caught Hydrolyzed Fish Collagen
Types 1 & 3 collagen from white fish

Glycine
Abundant amino acid found in collagen*

Proline
Amino acid involved in proteins biosynthesis

Hydroxyproline
Amino acid involved in collagen stabilization


Our oceans are a wonderful source of life. When we designed our marine collagen, we wanted the formula to represent the idea of purity, simplicity, and calmness. A glimpse of the wonders of marine life here on earth.
Pure marine collagen peptides powder of type I & III, sustainably sourced, and easy to use
Non-GMO. Meatless. Manufactured in the USA. 3rd party tested.
Wild-Caught, Cold Water White Fish Collagen.
Amino acid profile (average milligrams per serving): Alanine 765 mg, Arginine 954 mg, Aspartic Acid 423 mg, Glutamic Acid 873 mg, Glycine 1962 mg, Histidine 207 mg, Hydroxylysine 126 mg, Hydroxyproline 612 mg, Isoleucine 108 mg, Leucine 198 mg, Lysine 405 mg, Methionine 153 mg, Phenylalanine 189 mg, Proline 945 mg, Serine 540 mg, Threonine 333 mg, Tyrosine 45 mg, Valine 153 mg. Average milligrams per serving naturally occurring; absolute values may vary. Contains 8 of 9 essential amino acids. Not a significant source of protein. Collagen protein does not count toward the FDA recommended Percent Daily Value for protein because it lacks one essential amino acid: tryptophan. Packaged by weight, not volume. Settling may occur.
Adults take 1 scoop with 8-12 ounces of water or your favorite beverage or as directed by a qualified healthcare practitioner.
CAUTION: Do not exceed recommended dose. Pregnant, nursing mothers, children under 18 and individuals with a known medical condition should consult a physician before using this or any dietary supplement. Please use caution if you have allergies or sensitivities to any of the listed ingredients. Keep out of reach of children and pets. Do not use if safety seal is damaged or missing. Store in a cool dry place. Use this product as a food supplement only. Do not use for weight reduction.
Wild Caught Hydrolyzed Fish Collagen
Sanchez A, Blanco M, Correa B, Perez-Martin RI, Sotelo CG. Effect of Fish Collagen Hydrolysates on Type I Collagen mRNA Levels of Human Dermal Fibroblast Culture. Mar Drugs. 2018;16(5):144. Published 2018 Apr 26. doi: 10.3390/md16050144
König D, Oesser S, Scharla S, Zdzieblik D, Gollhofer A. Specific Collagen Peptides Improve Bone Mineral Density and Bone Markers in Postmenopausal Women-A Randomized Controlled Study. Nutrients. 2018;10(1):97. Published 2018 Jan 16. doi: 10.3390/nu10010097
Porfírio, Elisângela & Fanaro, Gustavo. (2016). Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: a systematic review. Revista Brasileira de Geriatria e Gerontologia. 19. 153-164. DOI: 10.1590/1809-9823.2016.14145
De Luca C, Mikhal'chik EV, Suprun MV, Papacharalambous M, Truhanov AI, Korkina LG. Skin Antiageing and Systemic Redox Effects of Supplementation with Marine Collagen Peptides and Plant-Derived Antioxidants: A Single-Blind Case-Control Clinical Study. Oxid Med Cell Longev. 2016;2016:4389410. doi: 10.1155/2016/4389410
Glynis A. A Double-blind, Placebo-controlled Study Evaluating the Efficacy of an Oral Supplement in Women with Self-perceived Thinning Hair. J Clin Aesthet Dermatol. 2012;5(11):28‐34. PMCID: PMC3509882
Proksch, E., Schunck, M., Zague, V., Segger, D., Degwert, J., & Oesser, S. (2014). Oral intake of specific bioactive collagen peptides reduces skin wrinkles and increases dermal matrix synthesis. Skin pharmacology and physiology, 27(3), 113–119. DOI: 10.1159/000355523
Proksch, E., Segger, D., Degwert, J., Schunck, M., Zague, V., & Oesser, S. (2014). Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. Skin pharmacology and physiology, 27(1), 47–55. DOI: 10.1159/000351376
Kumar, S., Sugihara, F., Suzuki, K., Inoue, N., & Venkateswarathirukumara, S. (2015). A double-blind, placebo-controlled, randomised, clinical study on the effectiveness of collagen peptide on osteoarthritis. Journal of the science of food and agriculture, 95(4), 702–707. DOI: 10.1002/jsfa.6752
Bello, A. E., & Oesser, S. (2006). Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders: a review of the literature. Current medical research and opinion, 22(11), 2221–2232. DOI: 10.1185/030079906X148373
Hexsel, D., Zague, V., Schunck, M., Siega, C., Camozzato, F. O., & Oesser, S. (2017). Oral supplementation with specific bioactive collagen peptides improves nail growth and reduces symptoms of brittle nails. Journal of cosmetic dermatology, 16(4), 520–526. DOI: 10.1111/jocd.12393
Glycine
Razak MA, Begum PS, Viswanath B, Rajagopal S. Multifarious Beneficial Effect of Nonessential Amino Acid, Glycine: A Review. Oxid Med Cell Longev. 2017;2017:1716701. doi: 10.1155/2017/1716701
Wang, W., Wu, Z., Dai, Z., Yang, Y., Wang, J., & Wu, G. (2013). Glycine metabolism in animals and humans: implications for nutrition and health. Amino acids, 45(3), 463–477. DOI: 10.1007/s00726-013-1493-1
Bannai M, Kawai N, Ono K, Nakahara K, Murakami N. The effects of glycine on subjective daytime performance in partially sleep-restricted healthy volunteers. Front Neurol. 2012;3:61. Published 2012 Apr 18. doi: 10.3389/fneur.2012.00061
De Paz-Lugo P, Lupiáñez JA, Meléndez-Hevia E. High glycine concentration increases collagen synthesis by articular chondrocytes in vitro: acute glycine deficiency could be an important cause of osteoarthritis. Amino Acids. 2018;50(10):1357-1365. doi: 10.1007/s00726-018-2611-x
Li, P., & Wu, G. (2018). Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth. Amino acids, 50(1), 29–38. DOI: 10.1007/s00726-017-2490-6
Kasznel, A. J., Zhang, Y., Hai, Y., & Chenoweth, D. M. (2017). Structural Basis for Aza-Glycine Stabilization of Collagen. Journal of the American Chemical Society, 139(28), 9427–9430. DOI: 10.1021/jacs.7b03398
Clements, K. A., Acevedo-Jake, A. M., Walker, D. R., & Hartgerink, J. D. (2017). Glycine Substitutions in Collagen Heterotrimers Alter Triple Helical Assembly. Biomacromolecules, 18(2), 617–624. DOI: 10.1021/acs.biomac.6b01808
Vieira, C. P., De Oliveira, L. P., Da Ré Guerra, F., Dos Santos De Almeida, M., Marcondes, M. C., & Pimentel, E. R. (2015). Glycine improves biochemical and biomechanical properties following inflammation of the achilles tendon. Anatomical record (Hoboken, N.J. : 2007), 298(3), 538–545. DOI: 10.1002/ar.23041
Vieira, C. P., Viola, M., Carneiro, G. D., D'Angelo, M. L., Vicente, C. P., Passi, A., & Pimentel, E. R. (2018). Glycine improves the remodeling process of tenocytes in vitro. Cell biology international, 42(7), 804–814. DOI: 10.1002/cbin.10937
Vieira, C. P., De Oliveira, L. P., Da Ré Guerra, F., Marcondes, M. C., & Pimentel, E. R. (2016). Green Tea and Glycine Modulate the Activity of Metalloproteinases and Collagen in the Tendinitis of the Myotendinous Junction of the Achilles Tendon. Anatomical record (Hoboken, N.J. : 2007), 299(7), 918–928. DOI: 10.1002/ar.23361
Proline
Vance L Albaugh, Kaushik Mukherjee, Adrian Barbul, Proline Precursors and Collagen Synthesis: Biochemical Challenges of Nutrient Supplementation and Wound Healing, The Journal of Nutrition, Volume 147, Issue 11, November 2017, Pages 2011–2017. DOI: 10.3945/jn.117.256404
Barbul A. (2008). Proline precursors to sustain Mammalian collagen synthesis. The Journal of nutrition, 138(10), 2021S–2024S. DOI: 10.1093/jn/138.10.2021S
Wu, G., Bazer, F. W., Burghardt, R. C., Johnson, G. A., Kim, S. W., Knabe, D. A., Li, P., Li, X., McKnight, J. R., Satterfield, M. C., & Spencer, T. E. (2011). Proline and hydroxyproline metabolism: implications for animal and human nutrition. Amino acids, 40(4), 1053–1063. DOI: 10.1007/s00726-010-0715-z
Hydroxyproline
Shigemura Y, Iwasaki Y, Tateno M, et al. A Pilot Study for the Detection of Cyclic Prolyl-Hydroxyproline (Pro-Hyp) in Human Blood after Ingestion of Collagen Hydrolysate. Nutrients. 2018;10(10):1356. Published 2018 Sep 22. doi: 10.3390/nu10101356
Qiu, B., Wei, F., Sun, X., Wang, X., Duan, B., Shi, C., Zhang, J., Zhang, J., Qiu, W., & Mu, W. (2014). Measurement of hydroxyproline in collagen with three different methods. Molecular medicine reports, 10(2), 1157–1163. DOI: 10.3892/mmr.2014.2267