Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

beta-D-Galactosidase (EC 3.2.1.23) was extracted from Streptococcus thermophilus grown in deproteinized cheese whey. Cultural conditions optimum for maximum enzyme production were pH 7.0, 40 degrees C, and 24 h. Proteose peptone (2.0%, wt/vol) and corn steep liquor (2.8%, wt/vol) were highly stimulatory, increasing the enzyme units available in their absence from 660 U/liter of medium to 18,200 and 10,000 U/liter of medium, respectively, in their presence. There was an insignificant increase in the production of enzyme in the presence of added inorganic nitrogen and phosphorus sources. Enzymatic hydrolysis for recuction of lactose content in aqueous solution and in skim milk was studied.
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PMID:Production of beta-galactosidase from Streptococcus thermophilus grown in whey. 2 Aug 40

The conditions and the intestinal processes responsible for the action of lactose as a potential dietary fibre are described. The beta-galactosidase activity in the rat caecum and colon is influenced by dietary factors: It declines with increasing lactose concentration and it rises with increasing protein and phosphate concentration in the diet. The enzyme activity correlates negatively with the content of lactose, and positively with the content of protein and phosphate in the chymus. The products of lactose hydrolysis are degraded by microbial glycolysis in caecum and colon. The glycolytic products are mainly absorbed and energetically utilized by the macroorganism. Phosphate stimulates the microbial metabolism and, therefore, accelerates the consumption of the energy substrate lactose. Mathematical optimization gives the necessary composition of the diet which causes an intended microecological effect. To minimize the chymus pH (5.1 in the colon ascendens; 4.6 in the colon descendens; 4.3 in the faeces) the lactose content of the diet has to be greater than or equal to 160 mumol/g, the protein content less than or equal to 10 mg/g, and the phosphate content less than or equal to 5.5 mumol/g. The minimal pH value depends to a greater extent on variations in the supply of protein and phosphorus with the diet whereas the response to changes in lactose concentration is less noticeable.
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PMID:[Lactose--a potential dietary fiber. The regulation of its microecologic effect in the intestinal tract. 4. Dietary fiber action of lactose: evaluation with multivariate statistical analysis]. 166 43

Female lactose adapted rats were kept for 10 days on human milk (HM), a milk diet adapted to human milk (MD1), and a milk diet rich in protein and phosphate (MD2), the lactose supply being always the same. In the caecum, colon and faeces, the pH value, the phosphorus content, the buffer capacity and the numbers of microorganisms with proteolytic activity (Bacteroides, Klebsiella, Proteus) were lower and the lactose concentration and the beta-galactosidase activity were higher on HM and MD1 than on MD2.
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PMID:[The degradation of lactose in the intestines of rats on human and cow's milk diets]. 647 40

Among 47 tested yeast strains, belonging to different genera, only two cultures of Kluyveromyces fragilis and Fabospora fragilis showed beta-galactosidase activity in shaken flasks. Three types of extraction were used to release the enzyme from K. fragilis cells: solvent and detergent extraction, freezing and thawing extraction, and mechanical disintegration prior to extraction, using Triton X-100. The results indicate that the highest yield could be obtained by mechanical disintegration of cells. Factors affecting the enzyme production were studied using fermentation media of different chemical composition. The medium containing lactose, salts and yeast extract with initial pH 7.0 was selected as the best for enzyme production. Monobasic ammonium phosphate (2.0 g/dm3) was found to be the best inorganic nitrogen source for enzyme production. The effect of phosphorus level was also studied.
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PMID:Selection of strain, culture conditions and extraction procedures for optimum production of beta-galactosidase from Kluyveromyces fragilis. 752 16

The syntheses and characterization of bisphenol A mono- and di-beta-D-glucopyranosides were undertaken to confirm that these compounds are major plant metabolities of bisphenol A (BPA) and to allow an assessment of their estrogenicity. Synthesis involved the glucosidation of unprotected BPA with glucose penta-acetate with phosphorus oxychloride as catalyst. The estrogenic activity of BPA and its mono- and di-beta-D-glucopyranosides were measured with an enzyme-linked immunosorbent assay (ELISA)-based estrogen receptor competitive binding assay and with a yeast two-hybrid assay adapted to a chemiluminescent reporter gene (for beta-galactosidase). Both methods showed that the estrogenicity of BPA was eliminated by formation of the di-glucoside, but whereas the ELISA-based method indicated that reduced activity remained in the monoglucoside, the yeast two-hybrid method showed the monoglucoside to be inactive. Presumably these results reflect the more complex interactions of test compound and cellular components required to demonstrate estrogenicity in the yeast two-hybrid assay. As these processes parallel those in mammalian cells, the yeast two-hybrid method is likely to be the more realistic assay. The uptake and metabolism of BPA by plants offers the possibility of phytoremediation of contaminated water, but also provides an additional route for the compound to enter the human food chain.
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PMID:Synthesis and estrogenic activity of bisphenol a mono- and di-beta-D-glucopyranosides, plant metabolites of bisphenol A. 1455 89

The hormonally active form of vitamin D(3),1alpha,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)], is synthesized in the kidney through a tightly regulated reaction catalyzed by 25-hydroxyvitamin D(3)-1alpha-hydroxylase (1alpha-hydroxylase), the product of the CYP27B1 gene. Through gene targeting in embryonic stem cells, we engineered a mouse strain in which the coding region of the 1alpha-hydroxylase gene is replaced by the genes for beta-galactosidase (lacZ) and neomycin resistance. Null mice produced no detectable 1alpha-hydroxylase transcript. The mice grew normally when maintained on a balanced diet containing 1,25(OH)(2)D(3) but rapidly developed rickets when phosphorus and 1,25(OH)(2)D(3) were restricted. Rickets was curable through administration of 1,25(OH)(2)D(3) but not its biological precursor, 25-hydroxyvitamin D(3). Upon administration of a diet low in calcium and devoid of any form of vitamin D(3), beta-galactosidase activity was detected in the kidneys of the -/- and +/- mice and in placentas harvested from -/- females bred with -/- males. No beta-galactosidase activity was detected in skin sections or in primary keratinocyte cultures from -/- animals. Our results demonstrate we have generated 1alpha-hydroxylase null mice that display phenotypes characteristic of vitamin D-dependency rickets type I. From the histochemical analysis of reporter gene expression in these mice, we conclude that acute 1,25(OH)(2)D(3) deficiency in otherwise healthy animals does not stimulate local production of 1,25(OH)(2)D(3) in the skin. These findings stand in contrast to previously published reports of 1,25(OH)(2)D(3) production in keratinocytes.
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PMID:CYP27B1 null mice with LacZreporter gene display no 25-hydroxyvitamin D3-1alpha-hydroxylase promoter activity in the skin. 1637 65

Protein bodies and spherosomes isolated from mature seeds of Sorghum bicolor (Linn.) Moench have measurable activity of acid protease, alpha-glucosidase, beta-glucosidase, beta-galactosidase, phytase, acid pyrophosphatase, p-nitrophenyl phosphatase, and RNase. Protein bodies have largely insoluble activities, and produce soluble protein and soluble amino nitrogen during autolysis. They have the dual function of protein storage and protein catabolism. Spherosomes have considerable amounts of soluble enzymes and autolytically produce soluble amino nitrogen and inorganic phosphate but release little soluble protein. Spherosomes are similar to animal lysosomes but have an additional storage function for protein, phosphorus, and metals. Mature sorghum seed contains the necessary enzymes and substrates to generate two basic metabolites, amino acids and inorganic phosphate.
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PMID:Acid Hydrolases and Autolytic Properties of Protein Bodies and Spherosomes Isolated from Ungerminated Seeds of Sorghum bicolor (Linn.) Moench. 1665 31