Archive for the ‘Amino Acids’ Category

The following is a review on a published article, “The Effect of Enzymes on Digestion.”, by Michael R. Bedford. Please note that his writings dealt with digestion in Birds.

Contrary to popular belief, that nutrients are always fully digested and absorbed in the blood stream, it is very unlikely that they ever do. Nutrients digestibilities vary between different dietary substances, however there are fours processes that help aid with digestibility. These four mechanisms are:

  • Deteriorating the cell wall 
  • Destroying ANF’s (supplements)
  • Supplying the Host’s Enzymes
  • Using intestinal bacteria

Destroying the cell wall.

Taken from www,newscenter.lbl,gov.

In this mechanism, Beta-glucanase, an enzymes, was used to break down the complex cell wall, rapidily allowing amylases and proteases to break down the cell’s content.

Getting rid of the ANF’s.

ANFs’ are supplements such as, non-starch polysaccharides, proteins, and amino acids.

It was observed that Beta-glucanase turned out to be soluble in barley. This was due to the Beta-glucan component being dissolved completely by the endosperm of the cell wall. ANF’s create viscosity, which reduces the effect of enzymes. Enzymes used to reduce intestinal viscosity are believed to improve digestion in the intestinal tract.

Viscosity. Taken from

Supplying the Host’s Enzymes.

Latest investigations has lead researchers to believe that the digestive tract may not have adequate enzymatic and absorption capacity to deal with all kinds of diets. However, work done by Bedford and Classen, proves that by adding the host enzymes, through means of supplements do in fact increase the rate at which these substances are digested.


Microbial presence?

The are millions of microbes present in your digestive tract. These microbes aid in digestion by breaking down the digestive substances to feed their own needs and produce, in some cases, helpful by products. Evidence to support the presence of microbes in our digestive tract is due to the presences of their by products in faeces.

Bacteria on the walls of the intestines


Bedford. Michael. R. 1996. ” The Effects of Enzymes on Digestion.” The Journal of Applied Poultry Research. Applied Poultry Inc, 1996. Accessed on April 11 2013.

Classen, H.L, T.A. Scotl, G.C. Irish, P. Hucl, M, and M.R Bedford, 1995.”The relationship of chemical and physical measurements to the apparent metabolize energy (AME) of wheat when fed to broiler chickens with and without and enzyme source”.Proc. of 2nd European Symp. on Feed Enzymes, Pages 65-77 Noordwijkerhout, NL. Accessed on April 11 2013.


A peptide bond (C-N) is formed when the α-amino group of one amino acid and the carboxyl group of the other amino acid combines, covalently, via condensation.



Peptides get their name from the peptide bonds between two or more amino acids. They are grouped accordingly to the number of amino acids found in the chain.

What makes an amino acid essential?

An essential amino acid is one that is not produced by the body and must be acquired through external means. A non-essential amino acid is made by the body, naturally and from the by-products of reactions.

Essential  Non-essential
Arginine Asparagine (from Aspartic Acid)
Histidine Aspartic Acid (from oxaloacetate)
Isoleucine Cysteine
Leucine Glutamine (from Glutamic Acid)
Lysine Glycine (from Serine or Threonine)
Methionine Proline (from Glutamic Acid)
Phenylalanine Serine (from glucose)
Threonine Tryosine ( from phenylalanine)
Trytophan Glutamic Acid (oxogluteric Acid)
Valine Alanine ( from pyruvic acid)

Amino Acids.

Posted: March 31, 2013 in Amino Acids
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Amino acids are made of up carbon, hydrogen, oxygen and nitrogen. They are monomers of all proteins. Every amino acid differs due to the R-group present.


There are four (4) classes of amino acids.

  1. Non-polar, aliphatic R groups, glycine, proline, valine and leucine, to name a few. Glycine is the smallest amino amino acid possible, having a hydrogen atom as the R-group. Proline is the most unique of this group as the R-group forms a ring structure, by connecting to the α-amino group. (Note: the α-amino group, although connected to the R-group, in proline, is not part of the R-group.)Image
  2. Aromatic R-groups. The term Aromatic comes from the presence of a bezene ring in the R-group. Example of these are Phenylalmine, Tryosine and Tryptophan.
  3. Positively charged R-groups. These are positively charged due to the positively charge on the nitrogen. For nitrogen to have a positive charge, it must have four other atoms bonded to it. Some examples of these are Lysine, Arginine and Histidine.
  4. Negatively Charged R-groups. Like positively charged amino acids, containing a positively charged amino group, negatively charged amino acids has an carboxyl group in the R-group, giving a negative charge. Examples are Aspartate and Glutamate.


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