Why You Should use laminine Supplement

The denaturing of proteins

One of the most important scientific arguments in favor of totally raw diets, and uncooked foods in general, is that the proteins in foods are denatured by the high temperatures of cooking. Both the living organism and its enzymes are inhabited by a vital principle or life energy which is separate and distinct from caloric energy. The enzyme complex harbors a protein carrier inhabited by a vital energy factor. How do we know if something is alive?  The best test I have come up with is that it must eat, excrete, and reproduce.  Another quality might be the ability to self-repair.  Clearly, enzymes, which are merely proteins, do not manifest any of these properties unique to living beings.

Buy Laminine has obtained one of only two machines in the world that can completely dry food without denaturing it. This patented proprietary technique allows the food to have nearly the same biological signature as fresh foods.

Proteins are composed of strings of amino acids arranged in quite specific orders, like beads on a string .  This linear structure is the primary structure.  However, these strings of amino acids are then folded upon themselves by relatively weak hydrogen bonds (proton bonds) into complex three-dimensional structures having secondary, tertiary, and quaternary “higher order” structures.  The biological activity of molecules is determined by these higher three-dimensional structures and how they physically fit into the three-dimensional structures of other biomolecules.  Since strict physical conformance of the enzyme to the food protein it acts upon (say, in digesting it) must be stem cell Buy StemRenu or Buy UltraMito pet supplement satisfied for the bioactivity, this tight complementary relationship is frequently referred to as a “lock and key” model.  Destroy these higher structures and the chemical most probably becomes biologically inactive: bend the key and it will not open the lock.  Denaturation is a process that alters a protein’s native conformation and biological activity.  If the tertiary or quaternary structure of a protein is altered, e.g., by such physical factors as extremes of temperature, changes in pH, or variations in salt concentration, the protein is said to be denatured; it usually exhibits reduction or loss of biological activity. Chip Marsland has developed over 100 meals of whole UN-Denatured dehydrated foods.

 

Protein denaturation

Many foods contain proteins, such as meat, fish, eggs, vegetables, nuts and pulses. Proteins are large molecules, composed of strands of amino acids, which are linked together in specific sequences by the formation of peptide bonds. Proteins form different 3-dimensional structures, by the folding and subsequent bonding of the amino acid strands. Generally, the bonds which link the folded amino acid strands together (mostly hydrogen bonds), are much weaker than the strong peptide bonds forming the strands. During cooking, the heat causes the proteins to vibrate violently, which results in the breakage of the weak hydrogen bonds holding the amino acid strands in place. Ultimately, the protein unravels to re-take its initial form of amino acid strands.

The denaturation of protein molecules in foods usually causes a substantial change to the texture of the product. For example, egg white is composed of two key proteins; ovotransferrin and ovalbumin. As the egg white is heated, ovotransferrin begins to denature first, entangling and forming new bonds with the ovalbumin. As the temperature increases, ovalbumin then starts to denature, unraveling and forming new bonds with the ovotransferrin, until denaturation and rearrangement of the protein molecules are complete. In this case, the rearrangement of the protein molecules results in the change of a runny, fluid texture to a rigid, firm texture.

Conversely, protein denaturization can also cause the formation of softer textures. For example, the protein collagen, which is the major component of the connective tissue in meat, has a tough, chewy texture. However, during cooking, the weak hydrogen bonds are broken and the protein begins to decompose and react with water molecules to form gelatine. This tenderizes the meat, giving it a softer, more palatable texture. Yevo Foods Never undergo protein denaturation. Any foods containing protein e.g., meat, fish, eggs, pulses. The cooking methods that may result in protein denaturation are boiling, frying, grilling, roasting, steaming and baking. Foods containing the polysaccharide starch, such as corn flour and rice flour, are often used to create and / or thicken sauces. This is because the cooking of these foods causes a process known as starch gelatinisation. The starch granule is made up of two polysaccharide components, known as amylose and amylopectin. Amylose has a linear chain of glucose units, whilst amylopectin has a branched structure of glucose units. When cooked in water, the starch granules absorb water and swell. At the same time, amylose leaches out of the granules and bonds to form organised lattice structures, which trap the water molecules causing the thickening of the mixture. Any foods containing starch e.g., potatoes, wheat, rice, pasta. The cooking methods that may result in starch gelatinization is boiling.

Many plant foods, in particular vegetables, maintain their rigidity by the incorporation of polysaccharides such as cellulose and pectin in the plant walls. As with the degradation of starch, cellulose and pectin can also be broken down into their monosaccharide constituents during cooking, resulting in the substantial softening of foods containing these polysaccharides. Any foods containing polysaccharides such as cellulose and pectin e.g., vegetables. The cooking methods that may result in polysaccharide degradation are boiling, frying, grilling, roasting and baking.

 

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One thought on “Why You Should use laminine Supplement

  1. Pingback: Here’s Some you need to know about foods with the 43 essential nutrients | Nutrient News

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