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)

Strain S22(T), a novel cellulolytic bacterium was isolated from the rhizosphere of pine trees. This isolate was Gram-reaction positive, motile and rods, and formed terminal or subterminal ellipsoidal spores. S22(T) represented positive activity for catalase, oxidase, esterase (C4), esterase lipase (C8), beta-galactosidase, leucine arylamidase, and hydrolysis of esculin. It contained meso-diaminopimelic acid as the diagnostic dia-mino acid in the cell-wall. The predominant isoprenoid quinone was menaquinone 7 (MK-7), and the major cellular fatty acids were anteiso-C(15:0) (52.9%), iso-Ci(16:0) (11.3%), and iso-C(15:0) (10.0%). The DNA G+C content was 43.3 mol%. Phylogenetic analysis based on 16S rRNA gene sequences showed that this isolate belonged to the family Paenibacillaceae. S22(T) exhibited less than 97.0% 16S rRNA gene similarity with all relative type strains in the genus Paenibacillus, and the most closely related strains were Paenibacillus anaericanus MH21(T) and Paenibacillus ginsengisoli Gsoil 1638(T), with equal similarities of 95.8%. This polyphasic evidence suggested that strain S22(T) should be considered a novel species in the genus Paenibacillus, for which the name, Paenibacillus pini sp. nov., is proposed. The type strain is S22(T) (=KCTC 13694(T) =KACC 14198(T) =JCM 16418(T)).
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PMID:Paenibacillus pini sp. nov., a cellulolytic bacterium isolated from the rhizosphere of pine tree. 2012 62

The purpose of this study was to evaluate the effect of high hydrostatic pressure (HHP) on the enzyme activities in Saccharomyces cerevisiae (ATCC 16664) and Escherichia coli (ATCC 11229). Enzyme activities before and after HHP treatment were determined using an APIZYME enzyme assay kit. Thirteen active enzymes were detected in S. cerevisiae and E. coli. Pressure treatment at 448 MPa for 30s at 23 degrees C resulted in different effects on enzymes in S. cerevisiae and E. coli. HHP completely inactivated lipase, cystine arylamidase, and chymotrypsin and moderately inactivated esterase, esterase lipase, leucine arylamidase, valine arylamidase and alpha-glucosidase in S. cerevisiae. In E. coli, esterase, esterase lipase, lipase, valine arylamidase, cystine arylamidase, trypsin, alpha-glucosidase, and beta-glucuronidase were completely inactivated and leucine arylamidase and beta-galactosidase retained partial activities. Phosphoric hydrolases were not inactivated in both microorganisms. The use of the enzyme assay kit provided rapid and useful information on the microorganisms' enzymes and their sensitivity to HHP treatment in a simple manner.
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PMID:Effect of high hydrostatic pressure on the enzyme activities in Saccharomyces cerevisiae and Escherichia coli. 2021 5

The anaerobic fungus Anaeromyces mucronatus KF8 grown in batch culture on M10 medium with rumen fluid and microcrystalline cellulose as carbon source produced a broad range of enzymes requisite for degradation of plant structural and storage saccharides including cellulase, endoglucanase, xylanase, alpha-xylosidase, beta-xylosidase, alpha-glucosidase, beta-glucosidase, beta-galactosidase, mannosidase, cellobiohydrolase, amylase, laminarinase, pectinase and pectate lyase. These enzymes were detected in both the intra- and extracellular fractions, but production into the medium was prevalent with the exception of intracellular beta-xylosidase, chitinases, N-acetylglucosaminidase, and lipase. Xylanase activity was predominant among the polysaccharide hydrolases. Extracellular production of xylanase was stimulated by the presence of cellobiose and oat spelt xylan. Zymogram of xylanases of strain KF8 grown on different carbon sources revealed several isoforms of xylanases with approximate molar masses ranging from 26 to 130 kDa.
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PMID:Xylanases of anaerobic fungus Anaeromyces mucronatus. 2068 May 72

The agar-degrading bacterium GNUM-1 was isolated from the brown algal species Sargassum serratifolium, which was obtained from the West Sea of Korea, by using the selective artificial seawater agar plate. The cells were Gram-negative, 0.5-0.6 micrometer wide and 2.0-2.5 micrometer long curved rods with a single polar flagellum, forming nonpigmented, circular, smooth colonies. Cells grew at 20 degrees C- 37 degrees C, between pH 5.0 and 9.0, and at 1-10% (w/v) NaCl. The DNA G+C content of the GNUM-1 strain was 45.5 mol%. The 16S rRNA sequence of the GNUM-1 was very similar to those of Alteromonas stellipolaris LMG 21861 (99.86% sequence homology) and Alteromonas addita R10SW13 T (99.64% sequence homology), which led us to assign it to the genus Alteromonas. It showed positive activities for agarase, amylase, gelatinase, alkaline phosphatase, esterase (C8), lipase (C14), leucine arylamidase, valine arylamidase, alpha-chymotrypsin, acid phosphatase, naphthol- AS-BI-phosphohydrolase, alpha-galactosidase, beta-galactosidase, beta-glucosidase, catalase, and urease. It can utilize citrate, malic acid, and trisodium citrate. The major fatty acids were summed feature 3 (21.5%, comprising C16:1omega7c/iso- C15:0 2-OH) and C16:0 (15.04%). On the basis of the variations in many biochemical characteristics, GNUM-1 was considered as unique and thus was named Alteromonas sp. GNUM-1. It produced the highest agarase activity in modified ASW medium containing 0.4% sucrose, but lower activity in rich media despite superior growth, implying that agarase production is tightly regulated and repressed in a rich nutrient condition. The 30 kDa protein with agarase activity was identified by zymography, and this report serves as the very first account of such a protein in the genus Alteromonas.
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PMID:Isolation and characterization of an agarase-producing bacterial strain, Alteromonas sp. GNUM-1, from the West Sea, Korea. 2322 23

BACKGROUND Cholesteryl ester storage disease (CESD), also known as lysosomal acid lipase deficiency (LAL-D), is a rare autosomal-recessive inheritable lysosomal storage disease. Since 2015, a causal treatment with sebelipase alfa, which replaces the missing LAL enzyme, has been approved. We report a fatal course of LAL-D in a female patient. CASE REPORT In 1979, CESD was first diagnosed in a 13-year-old female with marked hepatomegaly. At that time, no specific treatment for CESD was available and the spontaneous course of the disease had to be awaited. In 2013, a laparoscopic cholecystectomy for symptomatic gallstones was performed. The patient's CESD had caused a Child-Pugh A/B and Lab-MELD 14 cirrhosis with esophageal varices (grade III), a solitary fundal varix, as well as hepatosplenomegaly with thrombocytopenia. In 2016, the patient was admitted with compensated cirrhosis and splenomegaly for a ligature of esophageal varices which was complicated by vomiting of blood followed by severe coagulopathy and hemorrhagic shock. The dried blood test showed reduced acid lipase (0.03 nmol/spot*3 hours; reference range 0.2-2) and beta-galactosidase (0.08 nmol/spot*21 hours; reference range 0.5-3.2). Then 15 days after the esophageal varices bleed, the patient died due to multiorgan failure as a sequelae of advanced liver disease. CONCLUSIONS LAL-D should be included in the differential diagnosis of lipid metabolism disorder, hepatomegaly, and non-alcoholic fatty liver disease with fibrosis or cirrhosis. Causal treatment with sebelipase alfa should be introduced even in patients who have LAL-D and many years of clinically mild symptoms of this disease to prevent the serious sequelae of cirrhosis or cardiovascular complications.
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PMID:Cholesteryl Ester Storage Disease: Fatal Outcome without Causal Therapy in a Female Patient with the Preventable Sequelae of Progressive Liver Disease after Many Years of Mild Symptoms. 2977 83


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