Studies on the decarboxylation of amino acids by Brevibacterium linens
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منابع مشابه
Transport of aromatic amino acids by Brevibacterium linens.
Whole metabolizing Brevibacterium linens cells were used to study the transport of aromatic amino acids. Kinetic results followed the Michaelis-Menten equation with apparent Km values for phenylalanine, tyrosine, and tryptophan of 24, 3.5, and 1.8 microM. Transport of these amino acids was optimum at pH 7.5 and 25 degrees C for phenylalanine and pH 8.0 and 35 degrees C for tyrosine and tryptoph...
متن کاملFatty Acid Production from Amino Acids and -Keto Acids by Brevibacterium linens BL2†
Low concentrations of branched-chain fatty acids, such as isobutyric and isovaleric acids, develop during the ripening of hard cheeses and contribute to the beneficial flavor profile. Catabolism of amino acids, such as branched-chain amino acids, by bacteria via aminotransferase reactions and -keto acids is one mechanism to generate these flavorful compounds; however, metabolism of -keto acids ...
متن کاملProduction of S-Methylthioacetate by Brevibacterium linens.
Volatile sulfur compounds production by eight strains of Brevibacterium linens isolated from cheeses was demonstrated: methanethiol, dimethyldisulfide, and 2,3,4-trithiapentane. Four of these strains also produced S-methylthioacetate, an important aroma component of smear-coated cheeses. It is the first demonstrated microbiological production of a thioester.
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Synlett 2003, No. 4, Print: 12 03 2003. Art Id.1437-2096,E;2003,0,04,0542,0546,ftx,en;D28903ST.pdf. © Georg Thieme Verlag Stuttgart · New York ISSN 0936-5214 Abstract: Treatment of an α-amino acid with N-bromosuccinimide in water at pH 5 or in an alcoholic-aqueous ammonium chloride mixture, followed by addition of nickel(II) chloride and sodium borohydride, effected an overall decarboxylation v...
متن کاملSpectrophotometric Studies on the Decarboxylation of & Keto Acids
Reaction 1 is catalyzed by an enzyme widely distributed in animal tissues and present in some plants (1). Oxalacetic carboxylase, which catalyzes Reaction 2, has been found in bacteria (2), pigeon liver (3), and, to some extent, in other animal tissues as well as in plants (4). Mehler et al.’ have partially purified this enzyme from Microcowus lysocleikticus. Acetoacetic carboxylase (Reaction 3...
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ژورنال
عنوان ژورنال: Nihon Chikusan Gakkaiho
سال: 1969
ISSN: 1346-907X,1880-8255
DOI: 10.2508/chikusan.40.544