L-Tryptophane

L-Tryptophan is one of essential amino acids and the fourth limiting amino acid in animal diets, which means it could not be synthesized by the body, in addition, dietary supply through feed materials is usually insufficient.
The deficiency of L-Tryptophan was generally characterized as decreased feed intake and efficiency, and slow growth rate. Considering L-Tryptophan playing a key role in growth performance and feed efficiency, it is recommended to add L-Tryptophan in diet to achieve the optimal amino acid balance and fulfill the digestible tryptophan requirement of animals, especially piglets, sows and poultry etc.

L-Tryptophan is one of essential amino acids and the fourth limiting amino acid in animal diets, which means it could not be synthesized by the body, in addition, dietary supply through feed materials is usually insufficient.
The deficiency of L-Tryptophan was generally characterized as decreased feed intake and efficiency, and slow growth rate. Considering L-Tryptophan playing a key role in growth performance and feed efficiency, it is recommended to add L-Tryptophan in diet to achieve the optimal amino acid balance and fulfill the digestible tryptophan requirement of animals, especially piglets, sows and poultry etc.

Tryptophan is an essential amino acid which is the precursor of serotonin. Serotonin is a brain neurotransmitter, platelet clotting factor and neurohormone found in organs throughout the body. Metabolism of tryptophan to serotonin requires nutrients such as vitamin B6, niacin and glutathione. Niacin is an important metabolite of tryptophan. High corn or other tryptophan-deficient diets can cause pellagra, which is a niacin-tryptophan deficiency disease with symptoms of dermatitis, diarrhea and dementia. Inborn errors of tryptophan metabolism exist where a tumor (carcinoid) makes excess serotonin. Hartnup's disease is a disease where tryptophan and other amino acids are not absorbed properly. Tryptophan supplements may be useful in each condition, in carcinoid replacing the over-metabolized nutrient and in Hartnup's supplementing a malabsorbed nutrient. Some disorders of excess tryptophan in the blood may contribute to mental retardation. Assessment of tryptophan deficiency is done through studying excretion of tryptophan metabolites in the urine or blood. Blood may be the most sensitive test because the amino acid tryptophan is transported in a unique way. Increased urination of tryptophan fragments correlates with increased tryptophan degradation, which occurs with oral contraception, depression, mental retardation, hypertension and anxiety states. The requirement for tryptophan and protein decreases with age. Adults' minimum daily requirement is 3 mg/kg/day or about 200 mg a day. This may be an underestimation, for there are 400 mg of tryptophan in just a cup of wheat germ. A cup of low fat cottage cheese contains 300 mg of tryptophan and chicken and turkey contain up to 600 mg per pound.

Me gelek kargehên kalîteya bilind bi hevkariyek kûr heye, ku dikarin ji we re hilberên kalîteya bilind û bihayên reqabetê peyda bikin. Û em dikarin ji bo kirînên mezin erzanan jî bidin. Û em bi gelek pargîdaniyên barkêş ên profesyonel re hevkariyê dikin, dikarin hilberan bi ewlehî û bi aramî radestî destên we bikin. Dema radestkirinê piştî pejirandina dravdanê 3-20 rojan e.

What is tryptophan?

Tryptophan is one of essential amino acids and the fourth limiting amino acid in animal diets, which means it could not be synthesized by the body, in addition, dietary supply through feed materials is usually insufficient. The deficiency of L-Tryptophan was generally characterized as decreased feed intake and efficiency, and slow growth rate. Considering L-Tryptophan playing a key role in growth performance and feed efficiency, it is recommended to add L-Tryptophan in diet to achieve the optimalamino acid balance and fulfill the digestible tryptophan requirement of animals, especially piglets, sows and poultry etc.

Function of tryptophan

Tryptophan is an important precusor substance of auxin biosynthesis in plant. It has the similar structure of IAA. It widely exists in higher plant. There are two ways to synthetic auxin. The first is tryptophan oxidizes and deaminize and form indole acetone,then decarboxylation and form IAAId; Under the corresponding enzymes IAAId oxsidizes indoleacetic acid. The second way is decarboxylation and form to tryptamine then tryptamine oxsidize deamination finally forms tryptophan.

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