Takadiastase

Tait equation Takadiastase Takagi reagent Takahax process Takanelite Takasweet Takatherm... 

They prepared the acetate by means of acetic anhydride in dry pyridine and purified it by separation from an acetic acid solution to which warm methyl alcohol had been added n ]n2 = — 22.70° (c = 10, acetic acid), m. p. 206-208°. In the presence of barium hydroxide irisin formed an insoluble product whose composition was represented by 6(C6Hi0O6)-Ba(OH)2. In contrast to inulin, these authors found that Takadiastase at pH 5 to 5.5 did not hydrolyze irisin. 

Jokichi Takamine (1854-1922) went to the University of Glasgow, and then, to the United States to investigate the phosphatic manure, and he established the first company of phosphatic manure in Japan. He produced Takadiastase, a digestive agent containing various digestive enzymes, ribonuclease and cellulase. Amylase was extracted from Takadiastase. In a narrow sense, Takadiastase is one of the carboxyoroteases. He discovered in 1900. 

President of Chemical Society of Japan. Creator of physical chemistry of Japan. President of Japan Academy/the first president of JSPS, Baron Creation of industry of phosphatic manure. Discoverer of Takadiastase. Development of whisky in USA. Discoverer of Adrenaline... 

Either acid or alkaline hydrolysis can be applied, converting nicotinamide to nicotinic acid. Alkaline hydrolysis releases also the unavailable vitamers providing the estimation of the total niacin content. Acid hydrolysis, instead, is slower than alkaline hydrolysis therefore the former is usually coupled with enzymatic digestion by using takadiastase, papain, and clarase. Extraction with water and dilute sulfuric or hydrochloride acid has been applied to release the vitamers from the matrix without degrading nicotinamide [598]. 

Homogenization with HjO, glutathione, EDTA, citrate buffer, papain and takadiastase (for high starch samples) incubation over night filtration... 

Pantothenic acid occurs in foods both in the free form and bonded to coenzyme (CoA) or acyl carrier protein (ACP) therefore hydrolysis is needed to extract it totally. Since it is degraded by acid and alkaline hydrolysis, only an enzymatic digestion can be applied. Enzyme hydrolysis with papain, diastase, clarase, takadiastase, intestinal phosphatase, pigeon liver pantetheinase, or combination of them has been used. 

Extraction with 10% HCl at 80°C for 30 min centrifugation enzymatic digestion with takadiastase CM-cellulose column... 

Acid hydrolysis with PCA in ultrasonic bath enzymatic digestion with takadiastase and phosphatase centrifugation... 

Extraction is commonly carried out by hydrolysis in boiling acid such as chloridric acid or sulfuric acid. To release thiamine bonded to phosphate enzyme, hydrolysis with phosphatase, alone or together with claradiastase or takadiastase, is carried out. After the enzymatic digestion, an acid treatment is applied in order to precipitate the protein and denaturate the enzymes. Ndaw et al. [603] proved that for extraction of vitamins Bj, B, and Bg, acid hydrolysis is always superfluous if the activity of the enzymes chosen is sufficiently high. SPE or column chromatography may be used in further purification, mainly to remove excess of derivatization reagents used to convert thiamine to a highly flnorescent thiochrome derivatives. lEC may be used in purification step, as well. 

Vitamin Bg has been traditionally extracted by using acid hydrolysis (chloridric acid or sulfuric acid) at high temperature followed by enzymatic hydrolysis with takadiastase or phosphatase to release the phosphorilated vitamers. In the 1990s, a rapid method was proposed involving the transformation of all the vitamers into pyridoxol and then analyzed by ion pair chromatography [620], The following researches anyway focused the attention on separation and determination of all the different forms of vitamin B. ... 

Calf duodenal adenosine aminohydrolase affects enzymic hydrolysis of a wide variety of 6-substituted purine derivatives as well as analogs of adenosine with alteration in the purine ring and sugar moiety (Table IV) (65, 65a, 67, 70, 71, 112). Although not noted in Table IV, AMP, ADP, and ATP are not substrates. The hydrolysis of the 6-methoxy-purine derivative in H2180 occurs between C-6 and oxygen (113) consistent with the observed back incorporation of 180 from H2180 into inosine as catalyzed by both calf duodenal and Takadiastase non-... 

The reverse reaction, i.e., the direct conversion of inosine to adenosine catalyzed by both the calf duodenal and the Takadiastase nonspecific adenosine aminohydrolase (Section V) and measured as a function of pH with the calf enzyme, was defined by a theoretical curve for the equilibrium, K,= ([inosine] [NH i])/([adenosine] H20]) =38, with water concentration taken as one and pKa values of 8.8 and 9.2 for inosine and ammonium ion, respectively. The calculated AF = —5400 cal/mole at pH 7.0 was in reasonable agreement with —6000 cal/mole estimated from the summation of a series of partial reactions (114). 

Of the two homogeneous preparations of a nonspecific adenosine aminohydrolase from Aspergillus oryzae (Takadiastase) (92,179), that described by Wolfenden et al. (92) appears to be more facile and concise. Both procedures yield enzyme with turnover numbers near 105 moles adenosine deaminated per minute and molecular weights near 215,000. The mo-... 

Aspects of the mechanism of deamination catalyzed by the nonspecific Takadiastase enzyme are discussed in conjunction with calf duodenal adenosine aminohydrolase (see Section III). 

In 1957, RNase T, (5, 10, 11) was isolated from Takadiastase, a commercial product of Aspergillus oryzae (12). It is now a familiar enzyme used as an essential tool for the structural analysis of RNA. 

Recently, R. Fields, H. B. F. Dixon, and C. Yui (unpublished) have developed a chromatographic system for the isolation of RNase Tj. This procedure uses only a column of DEAE-cellulose equilibrated with a buffer of 0.08 M NaH2P04 and 0.12 M Na2HP04 after the water extraction of Takadiastase Y powder. 

Studies on microbial RNases began in 1924 when Noguchi found ribonucleic acid degrading enzymes in Takadiastase (134). Since then extensive studies have been carried out on RNA degrading enzymes. It is rather surprising that guanyloribonuclease so widely distributed in microorganisms was found only in 1957. This is because earlier studies did not consider base specificity. Even quite recently studies on nucleases or ribonucleases do not consider base specificity or do not separate nuclease mixtures from each other thus, information available on microbial RNases is still scant. 

Prepared samples of many types of food can be saponified directly. High-starch samples, such as breakfast cereals, may be digested with the enzyme takadiastase before saponification so as to avoid the formation of lumps (68). 

Total thiamine Baby food cereals cookies Acid hydrolysis with 0.1 M hydrochloric acid at 100°C for 30 min enzymatic hydrolysis of thiamine phosphates to thiamine with takadiastase at 47°C for 3 h weak ion-exchange (methyl-carboxylatein, add form) solid-phase extraction/ cleanup Analytical Lichrospher 100RP-18 (125 X 4 mm, 5 /u.m Merck ). Isocratic methanol + 10 mM phosphate buffer, pH 2.8 containing 5 mM sodium hexane-sulphonate + tri-ethylamine (15 + 84.9 + 0.1, v/v/v). 1.0 ml/min. UV absorbance 254 nm. External standardization. 79 Linear range = LoD to 7 /zg/ml thiamine, r = 0.9995. Reproducibility CV < 3% using food samples (n = 10). Recoveries 92.1-96.0% thiamine using baby food (n = 3). Samples spiked before hydrolysis. 

Due to the relative stability of the niacin vitamers, either acid or alkaline hydrolysis can be used to convert nicotinamide to nicotinic acid for quantitation of both vitamers as nicotinic acid (9,44). Acid hydrolysis is used to quantitate biologically available niacin. Alkaline hydrolysis releases both the biologically available and the unavailable vitamers and provides an estimate of the total niacin content. Because alkaline hydrolysis is much faster than acid hydrolysis, the latter is usually supplemented with enzymatic hydrolysis. The most common enzymes are takadiastase, papain, and clarase. On occasion, organic solvents such as methanol have been used to extract free nicotinic acid. 

Enzyme hydrolysis, with papain, diastase, clarase, takadiastase, intestinal phosphatase, or combinations thereof is most commonly used to release pantothenate from food proteins (186). A cold perchloric acid extraction was used to release pantothenic acid from tissue samples (187). Food spoilage prior to analysis may lead to inflated pantothenic acid levels (19). 

Treatment of hemicellulose-A from sapwood with Takadiastase, for 44 hours, caused the blue color (with iodine) to disappear, and yielded D-glu-... 

Hemicellulose-B(Table V) from sapwood gave a blue color with iodine, which disappeared after treatment with Takadiastase under carefully controlled conditions. The solution was found to contain n-glucose, and its reducing value was equivalent to 24.6% of hexosan. On the basis of analytical data, heartwood hemicellulose-B appeared to be similar in constitution to the polysaccharide (6 anhydro-n-xylose units and 1 0-methyl-hexuronic acid per structural unit) isolated- after prolonged enzymic hydrolysis of heartwood hemicellulose-A. 

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