PLUTOS ingredients are sourced locally in Europe.

Plutos Use Natural ingredients in Dog Chew Bone Bites
Best Chewy Bone Bites in Europe  for Dogs - Plutos


Milk Protein - Lactose free

Digestive Bone Chew

100% NATURAL flavors from certified suppliers: chicken, beef, chorizo, ham, salmon, lamb, duck and peanut butter

Long-Lasting Dog Chews Not Rawhide
Natural Beetroot Color Used in Dog Chews

100% NATURAL high-quality milk protein, lactose, and gluten-free. It takes a lot of effort to digest Casein protein, which in turn burns calories and speeds up our metabolism. It also creates a feeling of satiety which is a huge plus. On top of these factors, Casein is low in calories and has an extremely low level of fat. 

Casein protein is one of the two proteins that make up the dairy protein (the other being Whey protein). It is typically known as the 'slow' digesting component of milk protein

100% NATURAL colors from beetroot, carmine and anato

Recommended dosage, active amounts, other details

Like any protein supplement, casein protein supplements are dosed in relation to dietary protein goals and how much dietary protein is consumed via other sources. 

If your dog is highly active and currently you are attempting for him to lose body fat while preserving lean muscle mass, a daily intake of 1 chew, depending on its weight would be a good target (please see adequate chew size/dog weight size recommendation).

If your dog is sedentary and you are not looking for him to to change body composition, a weekly target of 2/3 chews  would be a good target.





Source and Components

1.1. Source

Casein is a protein that is derived from the milk of many species; most human consumption of casein comes from bovine (cow) milk.

Casein is the insoluble portion of the milk, whereas whey is the soluble portion; the amount of casein in standard milk protein is approximately 80%, and human milk is variable depending on time spent lactating.[1][2][3][4]


1.2. Components

Casein protein, like all protein, is a source of dietary amino acids. As it is an animal source, it is complete in the sense that it contains all essential amino acids in adequate enough numbers for proper human functioning at the minimum level of protein intake recommended.

Casein protein also contains various bioactive peptides. These peptides are partially digested in the stomach, and prior to being broken down into their constituent amino acids they are able to exert effects in the intestines (prior to absorption). These effects may be wide-reaching, and are discussed in the following bullets.

Like other dairy sources, Casein may  help your dental health. Studies have shown that it has the potential to strengthen tooth enamel against acid erosion and damage with its calcium, phosphate and hydroxide content.

List of Peptides in Casein

2.1. AlphaS-1 Peptide

Casein contains various Bioactive peptides, which can be defined as sequences of amino acids that are contained in dietary proteins and are partially denatured in the stomach to reveal short sequences. These sequences can exert biological effects in the intestines prior to being digested, or maybe digested through a peptide transporter.

When supplemented to humans, the AlphaS-1 peptide is known to produce an anxiolytic effect. Two doses of 200mg may be able to reduce the response to perceived stressors. The anxiolytic effect may also provide better sleep in those with high levels of stress.

Similar to the c12 peptide, AlphaS-1 may also have an ability to induce ACE-inhibitor like effects and reduce blood pressure.

AlphaS-1 is also a peptide that is noted to cause allergies, and thus persons allergic to dairy may also be allergic to this peptide in supplemental form.


2.2. c12 Peptide

When administered in the form of tablets, the c12 peptide is able to reduce blood pressure in pre-hypertensive subjects in one study.[20] This is due to the c12 peptide having the properties of an ACE inhibitor


2.3. Glycomacropeptides

Glycomacropeptides can be found in the casein portion of whole milk products, but due to their water soluble nature they leave the casein portion during chymosin treatment at the beginning stages of processing.[22] They do tend to be associated with casein protein as they originate with kappa casein molecules, hence their inclusion in this Examine page. Unless otherwise added afterwards however, they are not a normal component of casein supplementations.


2.5. Casoxins and Casomorphins

Casoxins and Casomorphins are peptides which are able to act on the opioid system, which is involved in the rate of digestion. The class of casomorphins are opioid agonists (activators) and the casoxins opioid antagonists.[23]

Casein seems to have a higher relative content of casomorphins to casoxins, which may explain the reduced transit speed after consumption (as activation of the opioid system reduces intestinal motility).[24]

Scientific Support & Reference Citations


  1. Kinsella JE. Milk proteins: physicochemical and functional properties. Crit Rev Food Sci Nutr. (1984)

  2. Lönnerdal B, Forsum E. Casein content of human milk. Am J Clin Nutr. (1985)

  3. Kunz C, Lönnerdal B. Re-evaluation of the whey protein/casein ratio of human milk. Acta Paediatr. (1992)

  4. Belloque J, Ramos M. Determination of the casein content in bovine milk by 31P-NMR. J Dairy Res. (2002)

  5. Kumar A, et al. Chymosin and other milk coagulants: sources and biotechnological interventions. Crit Rev Biotechnol. (2010)

  6. Johnson ME, Lucey JA. Major technological advances and trends in cheese. J Dairy Sci. (2006)

  7. Huffman LM, Harper WJ. Maximizing the value of milk through separation technologies. J Dairy Sci. (1999)

  8. Pastorino AJ, Hansen CL, McMahon DJ. Effect of salt on structure-function relationships of cheese. J Dairy Sci. (2003)

  9. Pastorino AJ, Hansen CL, McMahon DJ. Effect of pH on the chemical composition and structure-function relationships of cheddar cheese. J Dairy Sci. (2003)

  10. Lilbaek HM, et al. Improving the yield of Mozzarella cheese by phospholipase treatment of milk. J Dairy Sci. (2006)

  11. Everard CD, et al. Effects of cutting intensity and stirring speed on syneresis and curd losses during cheese manufacture. J Dairy Sci. (2008)

  12. Microfiltration in Cheese and Whey Processing.

  13. Solanki G, Rizvi SS. Physico-chemical properties of skim milk retentates from microfiltration. J Dairy Sci. (2001)

  14. Muro Urista C, et al. Review: Production and functionality of active peptides from milk. Food Sci Technol Int. (2011)

  15. Kim JH, et al. Efficacy of alphas1-casein hydrolysate on stress-related symptoms in women. Eur J Clin Nutr. (2007)

  16. Messaoudi M, et al. Effects of a tryptic hydrolysate from bovine milk alphaS1-casein on hemodynamic responses in healthy human volunteers facing successive mental and physical stress situations. Eur J Nutr. (2005)

  17. Guesdon B, et al. A tryptic hydrolysate from bovine milk alphaS1-casein improves sleep in rats subjected to chronic mild stress. Peptides. (2006)

  18. Rousseau-Ralliard D, et al. Inhibitory effect of αS1- and αS2-casein hydrolysates on angiotensin I-converting enzyme in human endothelial cells in vitro, rat aortic tissue ex vivo, and renovascular hypertensive rats in vivo. J Dairy Sci. (2010)

  19. Schulmeister U, et al. Cloning, expression, and mapping of allergenic determinants of alphaS1-casein, a major cow's milk allergen. J Immunol. (2009)

  20. Cadée JA, et al. Bovine casein hydrolysate (c12 Peptide) reduces blood pressure in prehypertensive subjects. Am J Hypertens. (2007)

  21. Townsend RR, et al. A randomized, double-blind, placebo-controlled trial of casein protein hydrolysate (C12 peptide) in human essential hypertension. Am J Hypertens. (2004)

  22. Keogh JB, et al. Effect of glycomacropeptide fractions on cholecystokinin and food intake. Br J Nutr. (2010)

  23. Teschemacher H, Koch G, Brantl V. Milk protein-derived opioid receptor ligands. Biopolymers. (1997)

  24. Taché Y, Garrick T, Raybould H. Central nervous system action of peptides to influence gastrointestinal motor function. Gastroenterology. (1990)

  25. Nakamura H, et al. Influences of casein hydrolysate ingestion on cerebral activity, autonomic nerve activity, and anxiety. J Physiol Anthropol. (2010)

  26. Messaoudi M, et al. Anxiolytic-like effects and safety profile of a tryptic hydrolysate from bovine alpha s1-casein in rats. Fundam Clin Pharmacol. (2009)