Efficient co-production of S -adenosylmethionine and glutathione by Candida utilis : effect of dissolved oxygen on enzyme activity and energy supply

2017 ◽  
Vol 92 (8) ◽  
pp. 2150-2158 ◽  
Author(s):  
Dechao Li ◽  
Dahui Wang ◽  
Gongyuan Wei
Keyword(s):  
Enzyme Activity ◽  
Dissolved Oxygen ◽  
Energy Supply ◽  
Candida Utilis

scholarly journals Occurrence of an endo-1,3-β-glucanase in culture fluids of the yeast Candida utilis. Purification and characterization of the enzyme activity

1979 ◽  
Vol 177 (1) ◽  
pp. 107-114 ◽  
Author(s):  
T G Villa ◽  
V Notario ◽  
J R Villanueva
Keyword(s):  
Enzyme Activity ◽  
Gel Electrophoresis ◽  
Candida Utilis ◽  
Culture Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Polyacrylamide Gel ◽  
Beta Glucanase ◽  
Hydrolysis Of

The endo-1,3-beta-glucanase (EC 3.2.1.6) secreted into the culture medium by cells of Candida utilis was isolated and purified to homogeneity on polyacrylamide-gel electrophoresis and in ultracentrifugation studies (s20,w = 1.97S). The purified enzyme represented only 0.001% of the total 1,3-beta-glucanase activity, the remainder being due to an exo-1,3-beta-glucanase enzyme, and behaved as an acidic glycoprotein (pI 3.3) in isoelectric-focusing experiments. The mol.wt. was estimated to be 21 000 by gel filtration and polyacrylamide-gel electrophoresis. Studies on the hydrolysis of different substrates showed that the enzyme was only able to break down (1 leads to 3)-beta-linkages, by an endo-splitting mechanism. Glucono-delta-lactone, D-glucoronolactone and heavy metal ions such as Hg2+ were inhibitors of the enzyme activity. The function of this endo-beta-glucanase in C. utilis is discussed.

AMIDE METABOLISM IN YEAST: III. ALIPHATIC AMIDE METABOLISM IN CANDIDA UTILIS

1961 ◽  
Vol 7 (4) ◽  
pp. 657-666 ◽  
Author(s):  
A. Domnas
Keyword(s):  
Fatty Acids ◽  
Enzyme Activity ◽  
Candida Utilis ◽  
Partial Purification ◽  
Ph Range ◽  
Ethylenediamine Tetraacetate ◽  
Aliphatic Amide

The partial purification and the properties of propionamide, valeramide, and hexanamide deamidases are described. The purified deamidases hydrolyzed propionamide, valeramide, and hexanamide to form ammonia and corresponding fatty acids. Maximum enzyme activity was obtained at 37 °C over a pH range of 6.7 to 7.8. The enzymes were inactivated at 55 °C in 10 minutes. Propionamide deamidase, the most potent deamidase, was inhibited by ethylenediamine tetraacetate, arsenite, and cyanide, and was partially inhibited by iodoacetamide.Evidence is presented which indicates the presence of more than one deamidase. Cell-free extracts hydrolyzed formamide, propionamide, valeramide, hexanamide. Lyophilized cells hydrolyzed acetamide, n- and iso-butyramide, iso-valeramide, and glycinamide. A procedure is described for separating propionamide deamidase from valeramide and hexanamide deamidases.

Effects of tetrahydrofuran on dissolved oxygen, pH, culturable aerobic microbes and enzyme activity in wastewater

2008 ◽  
Vol 90 (6) ◽  
pp. 1177-1186
Author(s):  
Zhenhua Lv ◽  
Yanlai Yao ◽  
Zhenmei Lv ◽  
Liya Sang ◽  
Hang Min
Keyword(s):  
Enzyme Activity ◽  
Dissolved Oxygen

scholarly journals Purification of an exo-β-D-glucanase from cell-free extracts of Candida utilis

1976 ◽  
Vol 159 (3) ◽  
pp. 555-562 ◽  
Author(s):  
V Notario ◽  
T G Villa ◽  
J R Villanueva
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Gel Electrophoresis ◽  
Candida Utilis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Polyacrylamide Gel ◽  
Acidic Amino Acids ◽  
Sepharose 4B ◽  
Hydrolysis Of

β-Glucanase present in cell-free extracts from Candida utilis was isolated and purified 562-fold by procedures that include adsorption on DEAE-Sephadex A-50 and filtration through columns of Sephadex G-50, G-100 and G-200, Bio-Gel P-10, and Concanavalin A-Sepharose 4B. The purified enzyme appeared homogeneous on polyacrylamide-gel electrophoresis and in ultracentrifugation studies (S20,w = 1.74S). The enzyme behaved as an acidic glycoprotein (pI4.1) with 68% carbohydrate and a high content of acidic amino acids. The mol.wt. was estimated to be 20000 from gel filtration and polyacrylamide-gel electrophoresis and 36000 from sedimentation experiments. Studies on the hydrolysis of different substrates showed that the enzyme is an unspecific β-glucanase able to break down both (1 leads to 3)-eta- and (1 leads to 6)-β-linkages by an exo-splitting mechanism. Glucono-δ-lactone, Zn2+ and Hg2+ inhibited the enzyme activity.

Evidence for regulatory trehalase activity in Candida utilis

1985 ◽  
Vol 31 (6) ◽  
pp. 529-537 ◽  
Author(s):  
J. C. Arguelles ◽  
M. Gacto
Keyword(s):  
Enzyme Activity ◽  
Stationary Phase ◽  
Candida Utilis ◽  
Fluoride Treatment ◽  
Trehalase Activity ◽  
Cell Extracts ◽  
In Vitro Activation ◽  
Regulatory Model

Candida utilis cells constitutively contain an acetate-insensitive intracellular trehalase (α,α-trehalose glycohydrolase; EC 3.2.1.28) whose activity is maximal during exponential growth. Cells grown on glucose, sucrose, or ethanol as carbon source show decreased levels of this trehalase activity as the cultures enter the stationary phase. The enzyme activity from stationary phase cells can be restored to the levels present in growing cells by preincubation of the cell extracts with adenosine 3′,5′-cyclic monophosphate and adenosine 5′-triphosphate. In vitro activation is also accomplished by addition of the catalytic subunit of a protein kinase preparation and adenosine 5′-triphosphate. The enzyme activity is enhanced in vivo by the presence of glucose or fluoride. Treatment of the trehalase with phosphatase results in a substantial loss of trehalase activity. Both activated and nonactivated trehalases show similar properties (Km = 1.01 × 10−2 M) and seem to be due to an enzyme with a molecular weight of 280 000. The data obtained are consistent with a regulatory model involving phosphorylation and dephosphorylation of the enzyme to control trehalase activity. In addition, another trehalase is present in this yeast whose activity is markedly inhibited by acetate.

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