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Biotin in food is bound to proteins. Digestive enzymes reduce the proteins to biotin-bound peptides. The intestinal enzyme biotinidase, found in pancreatic secretions and in the brush border membranes of all three parts of the small intestine, frees biotin, which is then absorbed from the small intestine. [4]
26 Σεπ 2024 · Biotin was first identified as a nutritive requirement of yeast. Originally called vitamin H, it was isolated in pure form in 1935; its structure was established in 1942, after it had been shown to be required by animals.
Biotin was discovered in nutritional experiments that revealed a factor in many food-stuffs that was capable of curing the scaly dermatitis, hair loss, and neurologic signs induced in rats fed dried egg whites. Avidin, a glycoprotein found in egg whites, binds biotin very specifically and tightly (Ka = 1015 mol/L) (1, 2).
Like many vitamins, biotin was "discovered" several times by different people and was given a new name by each of its discoverers. In the 1920s different researchers isolated a growth factor for yeast that some named "bios," and others called "vitamin H".
Biotin was discovered in nutritional experiments that revealed a factor in many foodstuffs that was capable of curing the scaly dermatitis, hair loss, and neurologic signs induced in rats fed dried egg whites. Avidin, a glycoprotein found in egg whites, binds biotin very specifically and tightly (Ka = 10 15 mol/L) (1, 2).
The aim was to describe the discovery of niacin, biotin, and pantothenic acid. By the 1920s, it became apparent that 'water-soluble B' (vitamin B) is not a single substance. In particular, fresh yeast could prevent both beriberi and pellagra, but the 'antipolyneuritis factor' in yeast is thermolabil ….
27 Οκτ 2022 · Biotin was initially discovered in 1927 in raw egg white, where it is bound to the protein avidin [1]. Even though it has been identified as a necessary nutrient for almost a century, it has only begun to be understood since the beginning of the twenty-first century.
