Testing of Micellar Casein, Blended Micellar Casein and Native Whey
Condition: Dietary Modification
Study type: Interventional

Summary: 
      The importance of protein in nutrition is momentous to ones health. Dietary proteins are
      essentially nutritional because they contain amino acids, which the body uses to build its
      own proteins, as well as other molecules that are essential for life. Protein when consumed,
      travels through your digestive system and is absorbed. They then enter the blood for
      transport to bodily tissues, and therefore, can be detected by blood sampling. There are
      differing amounts of each amino acid found in different types of protein supplements. Certain
      amino acids (the essential amino acids) are helping in stimulating muscle growth and helping
      to maintain muscle mass and function. It is important to understand how quickly these amino
      acids can be detected in your blood as well as how they affect blood glucose (blood sugar)
      and insulin activity. Understanding the effects of protein type on changes in levels of blood
      amino acids, glucose and insulin will provide helpful insight for the suggestion of
      supplement use.
    

Detailed description: 
      The importance of protein in nutrition is momentous to ones health. Dietary proteins are
      essentially nutritional because of their constituent amino acids, which the body uses to
      synthesize its own proteins, as well as nitrogen-containing molecules that are essential for
      life. The Recommended Dietary Allowance (RDA) for daily protein intake in healthy adults is
      0.8 g/kgBW/day. Younger individuals who participate in recreational or competitive
      activities, however, often attempt to go beyond the RDA by using protein supplements to help
      increase performance. For example, it was demonstrated that protein supplementation in
      conjunction with an eight-week resistance-training program elicited greater improvements in
      muscle hypertrophy and strength when compared to carbohydrate supplementation in untrained
      men. There were 3.2 to 17.5% increases in muscle cross-sectional area of the quadriceps
      femoris musculature and 14.5 to 30.3% strength gains in the leg extensors. Furthermore,
      several expert groups have recently advocated that certain individuals, such as older
      persons, should increase their daily intake to 1.0 to 1.5 g/kgBW/day to support the
      preservation of muscle and function. Other conditions also place greater than normal demands
      on amino acids, such as hypercatabolic stressed states, like that experienced by burn
      patients who's muscle protein breakdown rate increases by impairment to inward transmembrane
      transport of circulating blood amino acids. It was also found that an experimental enriched
      protein "medical food" comprised of 27% of calories as total protein resulted in postprandial
      increases in MPS rates for 5 hours by ∼33% (0.073 ± 0.023%∙h-1 to 0.097 ± 0.033%∙h-1) in
      advanced cancer patients. Thus, continually reassessing new and innovative nutrient therapies
      is necessary for extending the findings of existing studies after technological advances, and
      for providing nutritional support-to-support health.

      It is well known that dietary protein is a powerful transient stimulator of the muscle
      protein synthetic rate (MPS) whereby changes in MPS in response to feeding may be regulated
      by specific downstream target proteins of mammalian target of rapamycin signaling, such as
      S6K1, rpS6, and eIF2B. A meal deficient in protein, however, does not increase the rate of
      MPS because a rise in the bioavailability of amino acids does not occur. In addition, the
      source of dietary proteins has been shown to impact postprandial blood levels of amino acids.
      The concept that certain types of proteins are "fast acting" or "slow acting" has been shown
      to affect the postprandial profile of amino acids appearing in the systemic circulation.
      Native whey and micellar casein are both dairy proteins that contain a similar amount of
      essential (EAA), but blood EAA levels increase faster and to a higher level after the
      consumption of whey protein. Differences in gastric emptying, digestion and absorption
      kinetics between micellar casein and native whey are suggested to be the underlying factors.
      Nonetheless, micellar casein protein has been shown to protract MPS in humans. Despite the
      significant amount of information gained with respect to both of these protein sources, the
      effects of combinatorial formulations on the postprandial profile of amino acids appearing in
      the blood is less well known. The purpose of the present study is to test a novel blend of
      micellar casein combined with native whey to determine post-ingestion aminoacidemia,
      glycemia, and insulinemia in young adult men.
    

Intervention name(s): Testing of micellar casein, blended micellar casein and native whey, versus native whey to determine post-ingestion aminoacidemia, glycemia, and insulinemia in young adult men
Intervention type(s): Dietary Supplement
Intervention MeSH terms: Caseins
Allocation: Randomized
Intervention model: Crossover Assignment
Masking: Triple (Participant, Investigator, Outcomes Assessor)
Primary purpose: Treatment