They are the building blocks of proteins and hold significant importance in human nutrition and physiology. Our body's need for protein is essentially a need for amino acids. The proteins we consume daily from food are broken down into amino acids in the gastrointestinal tract through the action of enzymes like gastric proteases, pancreatic proteases, peptidases, and carboxypeptidases. These amino acids are then absorbed by the epithelial cells of the small intestine. Here are five main functions and components of amino acids:
- Synthesis or repair of tissue proteins: Amino acids are utilized to replenish the protein lost during the body's metabolic processes.
- Synthesis or conversion into other amino acids: For example, phenylalanine can be converted into tyrosine, and methionine can be synthesized into cysteine.
- Contribution to the process of amino acid breakdown metabolism, with the nitrogen-containing portion typically being transformed into urea.
- Formation of nitrogen-containing compounds outside of protein synthesis, such as purines and creatine.
- Acting as a source of metabolic fuel by releasing energy during the metabolic process to meet the body's needs.
Overall, amino acids play critical roles in maintaining human health and supporting various physiological functions.
There are approximately 175 different amino acids that have been isolated from various natural sources. However, only around 20 of these amino acids constitute the proteins in the human body. In order to meet the metabolic needs of the body, it is necessary for individuals to consume the essential amino acids through food intake. Among the over 20 amino acids that make up human protein, most can be synthesized directly within the body or converted from other amino acids. However, a few amino acids cannot be synthesized or are synthesized at a slow rate, which means they cannot meet the metabolic needs of the body. These amino acids are referred to as essential amino acids in nutrition. There are typically 8 essential amino acids: isoleucine, leucine, lysine, methionine, phenylalanine, threonine, valine, and tryptophan. Additionally, histidine is considered essential for infants.
The absorption of amino acids in the human body occurs in proportion to the metabolic needs of the body. Due to the specific proportions of amino acids that make up the proteins in human tissues, there are specific requirements for the quantity and proportion of each essential amino acid. For example, the body requires four times more leucine than tryptophan. If this balance is not maintained, it can lead to biological antagonistic effects, affecting protein synthesis and even causing nitrogen imbalance, where the total amount of nitrogen excreted in urine, feces, and sweat exceeds the nitrogen intake from diet. However, if the deficient essential amino acids are supplemented, the nitrogen balance required for proper metabolic function can be quickly restored.
Composition and function of essential amino acids
The proportion of 8 essential amino acids in a reference protein, as defined by the Food and Agriculture Organization (FAO) of the United Nations, is as follows: isoleucine 17.2%, leucine 12.9%, valine 14.1%, lysine 12.5%, methionine 10.7%, threonine 10%, phenylalanine 19.5%, and tryptophan 3.1%. In nutrition, proteins composed of amino acids with higher nutritional value and proportions that match the human body's needs are referred to as reference proteins.
If the composition of amino acids in a portion of food differs from the reference protein, the essential amino acid with the lowest content is called the limiting amino acid. If there are two or more amino acids that are deficient, they are ranked based on the degree of deficiency, known as the first limiting amino acid, second limiting amino acid, and so on. Animal protein foods have a composition of essential amino acids that closely match human requirements and do not contain any limiting amino acids. For example, egg whites contain 40% essential amino acids and are often considered an ideal reference protein.
However, plant protein foods have different proportions of the eight essential amino acids. They usually contain one limiting amino acid. For example, rice protein lacks sufficient lysine, followed by threonine and methionine, making lysine the first limiting amino acid in rice. Soy protein, on the other hand, has low levels of methionine, followed by threonine, making methionine the first limiting amino acid in soy protein.
An excess or deficiency of any essential amino acid in food can create a new imbalance between the required amino acids in the human body, and may even lead to negative nitrogen balance. Over time, this can affect physiological functions and result in metabolic disorders and decreased resistance of the body.
Maintaining an appropriate proportion of amino acids in the diet can be achieved through the following effective methods:
- Adjusting the diet rationally By utilizing the complementary effect of proteins, various foods can be combined to improve the balance and composition of amino acids, thereby enhancing the utilization value of proteins. For example, legume proteins have higher levels of lysine but are limited in certain amino acids compared to cereal foods. By combining legumes and cereals in appropriate proportions, their respective advantages can be utilized, making their nutritional value comparable to that of beef.
- Consuming foods fortified with essential amino acids appropriately When fortifying foods, it is important to prioritize the first, second, and third limiting amino acids in order; otherwise, it would be ineffective and may yield opposite results. For example, adding 0.2% lysine and 0.1% methionine to rice increases its protein's biological value from the original 1.5 to 2.6, and the protein digestibility increases from 50% to 70%, approaching the level of animal protein. Similarly, adding 0.5% methionine to soybeans can make the protein's nutritional value equivalent to that of meat, milk, and eggs.
- Moderately consuming some high-nutrient whole-protein foods Whole-protein foods, such as dairy products, eggs, lean meat, soybeans, and fish, contain a variety of essential amino acids in appropriate proportions, making them suitable for human needs. They are often referred to as high-quality protein sources.
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