Microbiology of domestic wastes. II. A comparative study of the seasonal physiological activity of bacteria indigenous to a sewage lagoon

1969 ◽  
Vol 15 (6) ◽  
pp. 563-569 ◽  
Author(s):  
Harvest Halvorson ◽  
M. Ishaque ◽  
H. Lees
Keyword(s):  
Comparative Study ◽  
Physiological Activity ◽  
Maximum Activity ◽  
Anaerobic Conditions ◽  
Egg Albumin ◽  
Lagoon Water ◽  
Surface Samples ◽  
Winter Conditions ◽  
Optimum Ph ◽  
Casamino Acids

A comparative study was made of the physiological activity of bacteria seasonally present in a sewage lagoon which experiences warm summers and very cold winters. Bacteria recovered from surface samples of lagoon water during summer were able to metabolize glucose, acetate, palmitate, creatinine, vitamin-free casamino acids, egg albumin, and urea aerobically at 25 °C, the highest prevailing temperature of the lagoon during summer. Under anaerobic conditions, acetate and palmitate were the only substrates not metabolized. Bacteria recovered from samples of lagoon water taken during winter were able to metabolize aerobically glucose, acetate, palmitate, creatinine, and urea at 2 °C, the prevailing temperature of lagoon water under ice cover, but casamino acids and egg albumin were not metabolized aerobically at 2 °C or 25 °C. Acetate, palmitate, casamino acids, and egg albumin were not metabolized anaerobically by bacteria in winter samples. Urea was hydrolyzed much more rapidly by bacteria in winter samples than by those present in summer samples and is probably the preferred nitrogen source for growth under winter conditions. The optimum pH for oxidation of acetate and casamino acids by bacteria in summer samples was 7.0; only 50% of the maximum activity was obtained at pH 9.0, virtually the highest pH that was found in the lagoon under natural conditions.The results show that bacteria active at low temperatures contribute appreciably to the stabilization of domestic wastes by the lagooning method even under severe winter conditions.

Microbiology of domestic wastes. I. Physiological activity of bacteria indigenous to lagoon operation as a function of seasonal change

1968 ◽  
Vol 14 (4) ◽  
pp. 369-376 ◽  
Author(s):  
Harvest Halvorson ◽  
M. Ishaque ◽  
H. Lees
Keyword(s):  
Temperature Change ◽  
Seasonal Change ◽  
Physiological Activity ◽  
Maximum Activity ◽  
First Year ◽  
Organic Substrates ◽  
Egg Albumin ◽  
Casamino Acids ◽  
Number Of Bacteria ◽  
Biodegradable Detergent

The physiological activity of bacteria indigenous to a mid-continental domestic wastes disposal unit (lagoon) was studied over a period extending from mid-May to the beginning of December, 1965. A rigorous climate induces a layer of ice over the lagoon for approximately 5 months of the year; this study entailed the interval under ice-free conditions during the first year of operation. Samples were collected roughly at weekly intervals and the activity of the bacteria free of algae was studied against several arbitrarily selected organic substrates. The activity was found to be a function of (a) the number of bacteria, (b) the temperature of the lagoon, and (c) the nature of the test substrate. The most rapid rates of oxidation occurred with casamino acids, acetate, and palmitate. Glucose, egg albumin, and Liqui-nox, a biodegradable detergent, were oxidized in a variable manner. Maximum activity occurred at 23 °C, the highest temperature reached by the lagoon during the summer. The rates of oxidation decreased markedly when the temperature decreased as a result of the onset of fall but all activities were not affected equally by the same temperature change.

scholarly journals Properties of pyruvate kinase and phosphoenolpyruvate carboxykinase in relation to the direction and regulation of phosphoenolpyruvate metabolism in muscles of the frog and marine invertebrates

1978 ◽  
Vol 174 (3) ◽  
pp. 979-987 ◽  
Author(s):  
Victor A. Zammit ◽  
Eric A. Newsholme
Keyword(s):  
Pyruvate Kinase ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Marine Invertebrates ◽  
Adductor Muscle ◽  
Sea Anemone ◽  
Anaerobic Conditions ◽  
Fructose Bisphosphate ◽  
Low Concentrations ◽  
Optimum Ph ◽  
Hill Coefficients

1. The properties of pyruvate kinase and, if present, phosphoenolpyruvate carboxykinase from the muscles of the sea anemone, scallop, oyster, crab, lobster and frog were investigated. 2. In general, the properties of pyruvate kinase from all muscles were similar, except for those of the enzyme from the oyster (adductor muscle); the pH optima were between 7.1 and 7.4, whereas that for oyster was 8.2; fructose bisphosphate lowered the optimum pH of the oyster enzyme from 8.2 to 7.1, but it had no effect on the enzymes from other muscles. Hill coefficients for the effect of the concentration of phosphoenolpyruvate were close to unity in the absence of added alanine for the enzymes from all muscles except oyster adductor muscle; it was 1.5 for this enzyme. Alanine inhibited the enzyme from all muscles except the frog; this inhibition was relieved by fructose bisphosphate. Low concentrations of alanine were very effective with the enzyme from the oyster (50% inhibition was observed at 0.4mm). Fructose bisphosphate activated the enzyme from all muscles, but extremely low concentrations were effective with the oyster enzyme (0.13μm produced 50% activation). 3. In general, the properties of phosphoenolpyruvate carboxykinase from the sea anemone and oyster muscles are similar: the Km values for phosphoenolpyruvate are low (0.10 and 0.13mm); the enzymes require Mn2+ in addition to Mg2+ for activity; and ITP inhibits the enzymes and the inhibition is relieved by alanine. These latter compounds had no effect on enzymes from other muscles. 4. It is suggested that changes in concentrations of fructose bisphosphate, alanine and ITP produce a coordinated mechanism of control of the activities of pyruvate kinase and phosphoenolpyruvate carboxykinase in the sea anemone and oyster muscles, which ensures that phosphoenolpyruvate is converted into oxaloacetate and then into succinate in these muscles under anaerobic conditions. 5. It is suggested that in the muscles of the crab, lobster and frog, phosphoenolpyruvate carboxykinase catalyses the conversion of oxaloacetate into phosphoenolpyruvate. This may be part of a pathway for the oxidation of some amino acids in these muscles.

Polygalacturonase isolated from the culture of the psychrophilic fungus Sclerotinia borealis

1997 ◽  
Vol 43 (5) ◽  
pp. 417-424 ◽  
Author(s):  
Toshihide Takasawa ◽  
Keiko Sagisaka ◽  
Koichi Yagi ◽  
Kyoko Uchiyama ◽  
Atsushi Aoki ◽  
...  
Keyword(s):  
Culture Medium ◽  
Enzyme Reaction ◽  
Wheat Seedling ◽  
Maximum Activity ◽  
Reducing Sugar ◽  
Pectic Acid ◽  
Snow Mold ◽  
Viscosity Change ◽  
Optimum Ph ◽  
Psychrophilic Fungus

A polygalacturonase was isolated from the culture medium of Sclerotinia borealis, a psychrophilic fungus that grows on lawn and wheat seedling under the snow in winter and induces the snow mold disease. Pectic acid was a better substrate of this enzyme than pectin when the activity was determined by measuring the reducing sugar produced. However, when the activity was measured by viscosity change, the viscosity of pectin decreased more rapidly than that of pectic acid. The results of viscosity change apparently indicate that the polygalacturonase catalyzes pectin hydrolysis as an endo-type enzyme. Highly methyl-esterified pectin was a poor substrate, as determined by measurements of reducing sugar production and viscosity change. It is suggested from the results that the methoxy group of pectin affects the polygalacturonase reaction. A reaction mechanism was proposed for the polygalacturonase reaction. Molecular mass of this enzyme was 40 kDa and its isoelectric point was pH 7.5. Optimum pH of the enzyme reaction was 4.5 and its optimum temperature was 40–50 °C. Thirty percent of the maximum activity was observed at 5 °C, but it was only slightly active above 60 °C. The activity was preserved for more than 2 years at 5 °C and pH 4.5, but it was lost when kept at room temperature overnight or heated at 50 °C for 30 min. The amino acid sequence of the N-terminal region of the psychrophilic polygalacturonase of Sclerotinia borealis is compared with those of polygalacturonases of mesophilic fungi. The function of this enzyme against the target plants is discussed with reference to the reaction of polygalacturonases of mesophilic fungi.Key words: polygalacturonase, pectin-hydrolyzing enzyme, psychrophilic fungi, snow mold disease, Sclerotinia borealis.

Rhabdothermus arcticus gen. nov., sp. nov., a member of the family Thermaceae isolated from a hydrothermal vent chimney in the Soria Moria vent field on the Arctic Mid-Ocean Ridge

2011 ◽  
Vol 61 (9) ◽  
pp. 2197-2204 ◽  
Author(s):  
Bjørn O. Steinsbu ◽  
Brian J. Tindall ◽  
Vigdis L. Torsvik ◽  
Ingunn H. Thorseth ◽  
Frida L. Daae ◽  
...  
Keyword(s):  
The Arctic ◽  
Rrna Gene ◽  
Organic Substrates ◽  
Mid Ocean Ridge ◽  
The Family ◽  
Optimum Ph ◽  
Casamino Acids ◽  
Ocean Ridge ◽  
Complex Organic ◽  
Acetate Butyrate

A novel thermophilic member of the family Thermaceae, designated strain 2M70-1T, was isolated from the wall of an active white smoker chimney collected in the Soria Moria vent field at 71 °N in the Norwegian–Greenland Sea. Cells of the strain were Gram-negative, non-motile rods. Growth was observed at 37–75 °C (optimum 65 °C), at pH 6–8 (optimum pH 7.3) and in 1–5 % (w/v) NaCl (optimum 2.5–3.5 %). The isolate was aerobic but could also grow anaerobically using nitrate or elemental sulfur as electron acceptors. The strain was obligately heterotrophic, growing on complex organic substrates like yeast extract, Casamino acids, tryptone and peptone. Pyruvate, acetate, butyrate, sucrose, rhamnose and maltodextrin were used as complementary substrates. The G+C content of the genomic DNA was 68 mol%. Cells possessed characteristic phospholipids and glycolipids. Major fatty acids constituted saturated and unsaturated iso-branched and saturated anteiso-branched forms. Menaquinone 8 was the sole respiratory lipoquinone. Phylogenetic analysis of 16S rRNA gene sequences placed the strain in the family Thermaceae in the phylum ‘Deinococcus–Thermus’, which is consistent with the chemotaxonomic data. On the basis of phenotypic and phylogenetic data, strain 2M70-1T ( = JCM 15963T  = DSM 22268T) represents the type strain of a novel species of a novel genus, for which the name Rhabdothermus arcticus gen. nov., sp. nov. is proposed.

scholarly journals Production of glucose and fructose syrups from cassava (Manihot esculenta Crantz) starch using enzymes produced by microorganisms isolated from Brazilian Cerrado soil

2010 ◽  
Vol 30 (1) ◽  
pp. 213-217 ◽  
Author(s):  
Roberto do Nascimento Silva ◽  
Fábio Pereira Quintino ◽  
Valdirene Neves Monteiro ◽  
Eduardo Ramirez Asquieri
Keyword(s):  
Aspergillus Niger ◽  
Manihot Esculenta ◽  
Glucose Isomerase ◽  
Cassava Starch ◽  
Maximum Activity ◽  
Brazilian Cerrado ◽  
Initial Activity ◽  
Manihot Esculenta Crantz ◽  
Streptomyces Sp ◽  
Optimum Ph

The high demands for sugars and the development of enzymatic technology have increased the production of sweeteners, especially for glucose and fructose syrups. This work describe a technology for glucose and fructose syrups from Brazilian cassava starch using enzymes produced by soil microrganisms isolated from the Brazilian Cerrado soil. Firstly, Aspergillus niger and Streptomyces sp. were isolated from the soil and used as glucoamylase (GA) and glucose isomerase (GI) producer sources. After characterization, GA and GI exhibited optimum pH 4.5 and 8.0, respectively. GA showed maximum activity at 60 ºC and GI at 85 ºC. GA and GI retained 65 and 80%, respectively, of initial activity after 180 minutes of incubation at 60 ºC. The kinetic parameters Km and Vmáx were 0.476 (mg.mL-1) and 8.58 (µmol/minute) for GA and 0.082 (M) and 48.20 (µmol/minute) for GI. The maximum glucose syrups production occurred after 24 hours of reaction with a 98% yield. The production of fructose syrups with 42% (w/v) was reached after 96 hours of reaction.

Cleavage of Canavaninosuccinic Acid by Human Liver To Form Guanidinosuccinic Acid, a Substance Found in the Urine of Uremic Patients

1969 ◽  
Vol 15 (5) ◽  
pp. 397-418 ◽  
Author(s):  
Kihachiro Takahara ◽  
Shigeko Nakanishi ◽  
Samuel Natelson
Keyword(s):  
Ascorbic Acid ◽  
Lipoic Acid ◽  
Human Liver ◽  
Liver Homogenate ◽  
Anaerobic Conditions ◽  
Optimum Ph ◽  
Reaction Proceeds ◽  
Uremic Patients ◽  
Guanidinosuccinic Acid ◽  
Intact Rats

Abstract Guanidinosuccinic acid (GSA) has been isolated in substantial quantities from the urine of uremic patients (1). Attempts to form this compound by transamidination from canavanine and arginine to aspartic acid were unsuccessful. A possible pathway has been found for GSA formation. Human liver homogenate splits canavaninosuccinic acid (CSA) to form homoserine and GSA. Optimum pH is at 8.7-8.8. The reaction proceeds best under anaerobic conditions. Reduced lipoic acid must be present for the reaction. NADH, NADPH, GSH, cysteine, ascorbic acid, NaCN, Fe++, and reduced CoA, dithiothreitol, and BAL cannot be substituted for the lipoic acid. BAL, NADH, NADPH, Fe++, and Co++ act as inhibitors for the reaction. A nondialyzable inhibitor also is present in the liver and can be washed out with water. More than 90% of GSA incubated with various tissues and administered subcutaneously to intact rats was recovered unchanged. It is suggested that GSA is an end product of metabolism in the human.

Glycosidases in bovine milk: α-mannosidase and its inhibition by zwitterions

1968 ◽  
Vol 46 (11) ◽  
pp. 1351-1356 ◽  
Author(s):  
A. Mellors ◽  
V. R. Harwalkar
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bovine Milk ◽  
Maximum Activity ◽  
Manganese Ions ◽  
Ammonium Sulfate Precipitation ◽  
Optimum Ph ◽  
High Concentrations ◽  
Hydrolysis Of ◽  
Dibasic Amino Acids

α-Mannosidase is present in bovine milk and is associated with the β-casein fraction following polyacrylamide gel electrophoresis. It was separated from the casein complex by ammonium sulfate precipitation in the presence of 10% (v/v) ethanol. Zinc or manganese ions are required for maximum activity and the enzyme is very labile. The optimum pH for the hydrolysis of p-nitrophenyl α-mannoside is about 3. In the presence of amino acid buffers the enzyme is inhibited. For dibasic amino acids this inhibition is inversely related to the [Formula: see text] of the amino acid and is apparently due to inhibition by zwitterions. High concentrations of the substrate p-nitrophenyl α-mannoside are inhibitory, and the apparent Km for this hydrolysis is 1.2 mM.

scholarly journals Nautilia nitratireducens sp. nov., a thermophilic, anaerobic, chemosynthetic, nitrate-ammonifying bacterium isolated from a deep-sea hydrothermal vent

2010 ◽  
Vol 60 (5) ◽  
pp. 1182-1186 ◽  
Author(s):  
Ileana Pérez-Rodríguez ◽  
Jessica Ricci ◽  
James W. Voordeckers ◽  
Valentin Starovoytov ◽  
Costantino Vetriani
Keyword(s):  
Gas Phase ◽  
Deep Sea ◽  
Hydrothermal Vent ◽  
Gene Sequence ◽  
Novel Species ◽  
Rrna Gene ◽  
East Pacific ◽  
Optimum Ph ◽  
Casamino Acids ◽  
The 16S Rrna Gene

A thermophilic, anaerobic, chemosynthetic bacterium, designated strain MB-1T, was isolated from the walls of an active deep-sea hydrothermal vent chimney on the East Pacific Rise at  ° 50′ N 10 ° 17′ W. The cells were Gram-negative-staining rods, approximately 1–1.5 μm long and 0.3–0.5 μm wide. Strain MB-1T grew at 25–65 °C (optimum 55 °C), with 10–35 g NaCl l−1 (optimum 20 g l−1) and at pH 4.5–8.5 (optimum pH 7.0). Generation time under optimal conditions was 45.6 min. Growth occurred under chemolithoautotrophic conditions with H2 as the energy source and CO2 as the carbon source. Nitrate was used as the electron acceptor, with resulting production of ammonium. Thiosulfate, sulfur and selenate were also used as electron acceptors. No growth was observed in the presence of lactate, peptone or tryptone. Chemo-organotrophic growth occurred in the presence of acetate, formate, Casamino acids, sucrose, galactose and yeast extract under a N2/CO2 gas phase. The G+C content of the genomic DNA was 36.0 mol%. Phylogenetic analysis of the 16S rRNA gene sequence indicated that this organism is closely related to Nautilia profundicola AmHT, Nautilia abyssi PH1209T and Nautilia lithotrophica 525T (95, 94 and 93 % sequence identity, respectively). On the basis of phylogenetic, physiological and genetic considerations, it is proposed that the organism represents a novel species within the genus Nautilia, Nautilia nitratireducens sp. nov. The type strain is MB-1T (=DSM 22087T =JCM 15746T).

Muscle Arylamidase Activity of Several Marine Species

1974 ◽  
Vol 31 (4) ◽  
pp. 445-449
Author(s):  
Beverly A. Bauer ◽  
R. R. Eitenmiller
Keyword(s):  
Blue Crab ◽  
Gel Electrophoresis ◽  
Marine Species ◽  
Maximum Activity ◽  
Crude Extracts ◽  
Muscle Extract ◽  
Optimum Ph

Arylamidase activity in muscle extracts of mackerel, mullet, whiting, blue crab, quahog clam, and shrimp was investigated. The optimum pH for activity was between 7.0 and 7.5 for each species using alanyl-β-naphthylamide as substrate. Enzymes of the three species of fish exhibited maximum activity against alanyl-β-naphthylamide, whereas the clam showed maximum activity with leucyl-β-naphthylamide and the crab and shrimp with lysyl-β-naphthylamide. Puromycin inhibited each of the arylamidases. Acrylamide gel electrophoresis of the crude extracts suggested the presence of one arylamidase in muscle of the fish, crab, and clam. The shrimp muscle extract contained two active enzymes. Upon electrophoresis, the faster moving enzyme from shrimp muscle was active against lysyl-, alanyl-, and leucyl-β-naphthylamides, but the slower moving enzyme was active only against lysyl-β-naphthylamide.

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