scholarly journals Differentiation of enzymatic activity of yeasts and yeast-like microorganisms isolated from various environments

2014 ◽  
Vol 35 (1) ◽  
pp. 53-60
Author(s):  
Elżbieta Bogusławska-Wąs ◽  
Waldemar Dąbrowski ◽  
Katarzyna Skoropada ◽  
Kinga Różycka-Kaszrelan
Keyword(s):  
Enzymatic Activity ◽  
Lipolytic Activity ◽  
Activity Level ◽  
Candida Lipolytica ◽  
Rhodotorula Rubra ◽  
Szczecin Lagoon ◽  
Trichosporon Beigelii

The aim of study was to determinate enzymatic activity of yeast-like organisms - <i>Candida lipolytica, Rhodotorula rubra, Trichosporon beigelii, Zygosaccharomyces</i> sp. - isolated from the Szczecin Lagoon and herring salads. We have shown that lipolytic activity was higher than protcolytic for every strain tested. The lowest activity level was found out for amylolytic hydrolases. The results also demonstrated that yeast-like organisms isolated from the Szczecin Lagoon revealed much higher average enzymatic activity compared to tbe same species isolated from herring salads, excepting <i>C. lipolytica</i>.

scholarly journals Activity of key enzymes involved in glucose and triglyceride catabolism during bovine oocyte maturation in vitro

Reproduction ◽  
2002 ◽  
pp. 675-681 ◽  
Author(s):  
P Cetica ◽  
L Pintos ◽  
G Dalvit ◽  
M Beconi
Keyword(s):  
Enzymatic Activity ◽  
Pentose Phosphate Pathway ◽  
In Vitro Maturation ◽  
Specific Activity ◽  
Lipolytic Activity ◽  
Cumulus Cells ◽  
Pentose Phosphate ◽  
Key Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

Little is known about the metabolic profile of cumulus-oocyte complexes (COCs) during maturation. The aim of this study was to determine the differential participation of enzymatic activity in cumulus cells and the oocyte during in vitro maturation of bovine oocytes, by measuring the activity of key enzymes involved in the regulation of glycolysis (phosphofructokinase), the pentose phosphate pathway (glucose-6-phosphate dehydrogenase) and lipolysis (lipase). COCs were matured in medium 199 plus 10% (v/v) steer serum for 22-24 h at 39 degrees C in 5% CO(2):95% humidified air. Phosphofructokinase, glucose-6-phosphate dehydrogenase and lipase activities were measured in immature and in vitro matured COCs, denuded oocytes and cumulus cells, respectively. Phosphofructokinase and glucose-6-phosphate dehydrogenase activities (enzymatic units) remained constant during in vitro maturation of COCs, but there was a significant decrease in lipase activity (units) (P < 0.05), as activity in cumulus cells decreased significantly (P < 0.05). For the three enzymes studied, enzyme activity (units) remained unchanged in the oocyte during in vitro maturation. Specific activity increased in the oocyte (P < 0.05) and decreased in cumulus cells as a result of maturation (P < 0.05). In cumulus cells, phosphofructokinase was the most abundant of the three enzymes followed by glucose-6-phosphate dehydrogenase and then lipase (P < 0.05), whereas in the denuded oocyte this order was reversed (P < 0.05). Thus, the metabolism of cumulus cells is adapted to control the flow of metabolites toward the oocyte, which maintains its enzymatic activity even when dissociated from cumulus cells during maturation. The high activity of phosphofructokinase in cumulus cells indicates that glucose is metabolized mainly via the glycolytic pathway in these cells. The greater relative activity of glucose-6-phosphate dehydrogenase recorded in the oocyte indicates that glucose uptake could be directed mainly toward the pentose phosphate pathway. The marked lipolytic activity concentrated in the oocyte indicates an active participation in lipid catabolism during maturation.

scholarly journals Ecological features of enzyme activity distribution in edaphotops of technogenic landscapes

2018 ◽  
Vol 29 (2) ◽  
Author(s):  
V. I. Chorna ◽  
I. V. Wagner ◽  
V. V. Katsevych
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
High Efficiency ◽  
Soil Column ◽  
Hydrolytic Enzyme ◽  
Activity Level ◽  
Artificial Soil ◽  
Soil Enzymatic Activity ◽  
Ecological Features

Specific features of distribution total, available phosphorus concentrations and levels of phosphatase enzymatic activity at the layers of artificial soil, sod-lithogenic soils onto gray-green and red-brown clays and on loess-like loams in the Nikopol manganese ore basin are established. It is presented general assessment of technosoil status by evaluation of phosphatase enzyme activity; this enzyme enriches the soil with mineral phosphorus and thereby improves its availability for living organisms. Among current bioindication methodology, soil enzymatic method is the most reliable and promising because enzymatic activity serves a stable indicator of soil biogenicity in comparison with other indicators. Soil enzymatic activity determines both intensity and targeting of biogeochemical processes. High correlation between concentrations of soluble phosphorus and phosphatase activity values by layers of artificial soil (r = 0.87), sod-lithogenic soils onto gray-green (r = 0.77), red-brown clays (r = 0.62) and onto loess-like loam (r = 0.95) was determined. Tendency of decreasing hydrolytic enzyme activity, phosphatase, with depth in all types of artificial soil studied was established. High efficiency of the enzymatic activity study in diagnostics of soil fertility dynamics under impact of various anthropogenic and natural ecosystems was determined. Advantages of using this method are capability to determine rapidly the changes occurring in ecosystems in the early stages of degradation processes and prediction of their targeting and, accordingly, their intensity. It has been found that levels of phosphatase activity and values of mobile phosphorus compounds in complex biogeocoenotic systems are sensitive quantitative indicators of changes in environmental conditions in man-made environment, and they generate good data about processes occurred within the soil column. The use of phosphatase activity level can be a reliable and promising method on biomonitoring of technogenic edaphotops.

DETERIORAÇÃO DE REFRIGERANTES POR LEVEDURAS

2004 ◽  
Vol 5 (2) ◽  
Author(s):  
C. D. Rocha ◽  
H. J. Schmidt ◽  
C. Monteiro ◽  
E. Odebrecht
Keyword(s):  
Soft Drink ◽  
Debaryomyces Hansenii ◽  
Rhodotorula Glutinis ◽  
Cryptococcus Laurentii ◽  
Rhodotorula Mucilaginosa ◽  
Candida Lipolytica ◽  
Rhodotorula Rubra ◽  
Zygosaccharomyces Bailii ◽  
Candida Sp ◽  
Saccharomycodes Ludwigii

Refrigerantes são bebidas não alcoólicas carbonatadas e constituem ótima fonte de glicídios. A composição química adocicada, o pH menor que 4,3, a aw maior que 0,90 e a atmosfera dos refrigerantes oferece condições favoráveis ao desenvolvimento de diversos microrganimos, incluindo leveduras deteriorantes..A deterioração ocasionada nos refrigerantes não constitui um risco à saúde das pessoas, mas este fenômeno prejudica a imagem de fábricas de refrigerantes, como também pode causar sérias perdas econômicas..Essas perdas podem ser minimizadas com o rastreamento da origem dos focos de contaminação, bem como conhecendo o risco potencial que cada levedura representa para o produto..As leveduras comumente detectadas em bebidas não alcoólicas carbonatadas, são as Brettanomyces sp, Candida lipolytica, Candida sp, Criptococcus albidus, Cryptococcus laurentii, Debaryomyces hansenii, Hanseniaspora sp, Hansenula sp, Kloeckera sp, Kluyveromyces sp, Zygosaccharomyces bailii, Zygosaccharomyces rouxii, Rhodotorula mucilaginosa, Rhodotorula glutinis, Rhodotorula rubra, Pichia sp, Saccharomyces cerevisae, Saccharomyces sp.,Saccharomycodes ludwigii, Schizosaccharomyces sp, e Zygosaccharomyces sp. SOFT DRINK DETERIORATION BY YEASTS Abstract Soft drinks are non alcoholic carbonated beverages that become an excellent source of glycids. Sugar composition, pH lower than 4.3, aw higher than 0.90 and atmosphere of soft drinks are conditions that contribute for the development of many microorganisms, including spoilage yeasts. Soft drink deterioration is not a health risk for people, but this phenomenon damages the beverage companies image and can yield serious economic damages. This problem could be reduced knowing the contamination focus origin, and also understanding the potential risk that each yeast represents to the product. The common yeasts found in nonalcoholic carbonated beverages are Brettanomyces sp, Candida lipolytica, Candida sp, Criptococcus albidus, Cryptococcus laurentii, Debaryomyces hansenii, Hanseniaspora sp, Hansenula sp, Kloeckera sp, Kluyveromyces sp, Zygosaccharomyces bailii, Zygosaccharomyces rouxii, Rhodotorula mucilaginosa, Rhodotorula glutinis, Rhodotorula rubra, Pichia sp, Saccharomyces cerevisae Saccharomyces sp, Saccharomycodes ludwigii, Schizosaccharomyces sp and Zygosaccharomyces sp.

scholarly journals Comparison of enzymatic activity of selected yeast-like fungi isolated from lakes and astatic reservoirs

2014 ◽  
Vol 33 (1) ◽  
pp. 37-42
Author(s):  
Maria Dynowska ◽  
Anna Biedunkiewicz
Keyword(s):  
Candida Albicans ◽  
Chemical Composition ◽  
Enzymatic Activity ◽  
Morphological Differentiation ◽  
Water Reservoirs ◽  
Physiological Differences ◽  
Trichosporon Beigelii

The stains of <i>Candida albicans</i> and <i>Trichosporon beigelii</i> isolated from astatic reservoir show a higher enzymatic activity than the strains isolated from lake. The results obtained confirm earlier suspicions that the morphological differentiation of micro-fungi living in different water reservoirs is generally accompanied by physiological differences, which arc, to the largest extent, reflections of the chemical composition of the environment.

290 ENZYMATIC ACTIVITY LEVEL OF SOME GLYCOSIDASES IN BOVINE OVIDUCTAL FLUID AT DIFFERENT STAGES OF THE ESTROUS CYCLE

2007 ◽  
Vol 19 (1) ◽  
pp. 260 ◽  
Author(s):  
C. Carrasco ◽  
R. Romar ◽  
J. Marcos ◽  
M. Aviles ◽  
P. Coy
Keyword(s):  
Enzymatic Activity ◽  
Corpus Luteum ◽  
Estrous Cycle ◽  
Luteal Phase ◽  
Reproductive Tract ◽  
Total Activity ◽  
Activity Level ◽  
Cycle Phase ◽  
Activity Levels ◽  
Oviductal Fluid

Carbohydrates play a key role in different reproductive events such as the sperm–oviductal cell interaction and sperm–oocyte recognition. In this way, α-d-mannosyl (Amari et al. 2006 Mol. Reprod. Dev. 59, 221–226) and α-2,3-sialic acid (Velasquez et al. 2006 Mol. Reprod. Dev. in press) residues contained in the zona pellucida have been identified as sperm receptors in bovine oocytes. The glycosidases, enzymes that remove carbohydrates, could play an important role in the reproductive tract, modulating decisive physiological events mediated by carbohydrates. However, the enzymatic activity level of these enzymes or its fluctuations throughout the estrous cycle in the bovine oviductal fluid (BOF) has not been studied. The objective of this work was to compare the enzymatic activity level of 7 different glycosidases in the oviductal fluid of cows at different stages of the estrous cycle. Oviducts were collected from the abattoir and classified according to the macroscopic aspect of the genital tract (Grippo et al. 1995 J. Reprod. Fertil. 105, 57–64) as early follicular (presence of growing follicles), late follicular (presence of a dominant follicle), early luteal phase (ovaries showing a corpus hemorrhagicum or a recent corpus luteum), and late luteal phase (old corpus luteum or corpus albicans). Oviductal fluid samples were collected by aspiration with an automatic pipette making simultaneous manual pressure from the isthmus toward the ampulla. Samples (9 per group) were centrifuged (7000g, 10 min) and supernatant was stored at −20°C until assay. Total activity levels were fluorimetrically measured at 450 nm, with the corresponding substrate conjugated to 4-methylumbelliferil for each enzyme (Abascal et al. 1998 Biochem. J. 333, 201–207) using a fluorometer Fluostar Galaxy (BMG LABTECH GmbH, Offenberg, Germany). Enzymatic assays were done in duplicate for 4 h at 37°C, and the reactions were stopped by adding glycine-calcium carbonate buffer. Fluorescences were corrected for tissue and substrate blanks. Fluorescence results of each enzyme and oviduct phase were analyzed using a 1-way ANOVA, with estrous cycle phase being the main factor. Results (mean counts of fluorescence) showed that the level of activity changes during the estrous cycle and the activity of some enzymes increases close to or after ovulation, suggesting a role of some glycosidases in the fertilization process. Preliminary assays for neuraminidase were negative for all samples. Future studies are necessary to identify the biological role played by the glycosidases present in the bovine oviductal fluid. Table 1.Enzymatic activity level of some glycosidases in bovine oviductal fluid at different stages of the estrous cycle This work was supported by Fundación Séneca (03018/PI/05) and MEC (Project code 3495).

Fate of pancreatic enzymes during small intestinal aboral transit in humans

1986 ◽  
Vol 251 (4) ◽  
pp. G475-G480 ◽  
Author(s):  
P. Layer ◽  
V. L. Go ◽  
E. P. DiMagno
Keyword(s):  
Enzymatic Activity ◽  
Structural Integrity ◽  
Amylase Activity ◽  
Lipolytic Activity ◽  
Pancreatic Insufficiency ◽  
Exocrine Pancreatic Insufficiency ◽  
Pancreatic Enzymes ◽  
Trypsin Activity ◽  
Tryptic Activity ◽  
Small Intestinal

To determine survival of pancreatic enzymes during small intestinal aboral transit in humans, seven healthy volunteers were intubated with an oroileal tube. By using nonabsorbable markers we measured the cumulative amount of lipase, trypsin, and amylase activities and lipase and trypsin immunoreactivities delivered postprandially to the duodenum, midjejunum, and terminal ileum. We found that as the enzymes moved from duodenum to ileum, 74% of amylase activity, 22% of trypsin activity, and 1% of lipase activity survived transit. Enzymatic activity and immunoreactivity of trypsin and lipase disappeared at different rates, suggesting that for these enzymes the sites of enzymatic activity and immunorecognition are not identical. Since tryptic activity is present even in the absence of immunorecognizable trypsin, complete structural integrity of the trypsin molecule may not be essential for its enzymatic activity. The short intraluminal survival of lipolytic activity may partially explain why patients with progressive exocrine pancreatic insufficiency malabsorb fat earlier than other nutrients.

310 DETERMINATION OF THE PORCINE OVIDUCTAL GLYCOSIDASES DURING THE ESTROUS CYCLE

2007 ◽  
Vol 19 (1) ◽  
pp. 270 ◽  
Author(s):  
R. Romar ◽  
C. Carrasco ◽  
J. Marcos ◽  
M. Avilés ◽  
P. Coy
Keyword(s):  
Enzymatic Activity ◽  
Estrous Cycle ◽  
Luteal Phase ◽  
Reproductive Tract ◽  
Total Activity ◽  
Activity Level ◽  
Cycle Phase ◽  
Corpora Lutea ◽  
Activity Levels ◽  
Oviductal Fluid

Carbohydrates play a key role in different reproductive events, such as the sperm–oviductal cell interaction and sperm–oocyte recognition. For example, β-d-galactose and α-d-mannose residues contained in the zona pellucida have been identified as sperm receptors in porcine oocytes (Song et al. 1999 J. Mamm. Ova Res. 16). The glycosidases, enzymes that remove carbohydrates, could play an important role in the reproductive tract, modulating decisive physiological events mediated by carbohydrates. However, the enzymatic activity level of these enzymes or their fluctuations throughout the estrous cycle in the porcine oviductal fluid (POF) has not been studied. The objective of this work was to compare the enzymatic activity level of 7 glycosidases in the POF at different stages of the estrous cycle. Oviducts were collected from the abattoir and classified according to the macroscopic aspect of the genital tract (Grippo et al. 1995 J. Reprod. Fertil. 105, 57–64) as early follicular please (presence of growing follicles), late follicular phase (presence of several grown follicles), early luteal phase (ovaries showing corpora hemorrhagica or recent corpora lutea), and late luteal phase (old corpora lutea or corpora albicans). After classification, oviducts were dissected and oviductal fluid samples were collected by aspiration with an automatic pipette while applying manual pressure from the isthmus toward the ampulla. Samples (6 per group) were centrifuged (7000g, 10 min) and the supernatant was stored at −20°C until assay. Total activity levels were measured fluorimetrically at 450 nm with the corresponding substrate conjugated to 4-methylumbelliferyl for each enzyme (Abascal et al. 1998 Biochem. J. 333, 201–207) using a FLUOstar Galaxy fluorometer (BMG Lab Technologies, Offenburg, Germany). Enzymatic assays were done in duplicate for 4 h at 37°C, and the reactions were stopped by adding glycine–calcium carbonate buffer. Fluorescence was corrected for tissue and substrate blanks. Fluorescence results of each enzyme and oviduct phase were analyzed using a one-way ANOVA with estrous cycle phase being the main factor. Results (mean counts of fluorescence, see Table 1) showed that changes of enzymatic activity during the estrous cycle and activity of some enzymes were modified during or after ovulation, suggesting a role of some glycosidases in the fertilization process. Preliminary assays for neuraminidase were negative in all samples. Future studies are necessary to identify the biological role played by the glycosidases present in the POF. Table 1.Changes in porcine oviductal glycosidases during the estrous cycle Supported by Fundacion Seneca (03018/PI/05) and Ministerio de Educacío y Ciencia (Project code 3495).

scholarly journals Partial purification, characterization and immobilization of a novel lipase from a native isolate of Lactobacillus fermentum

2021 ◽  
Author(s):  
Foruzan Fathi ◽  
Rouha Kasra-Kermanshahi ◽  
Zahra Moosavi-Nejad ◽  
Elahe Mobarak Qamsari
Keyword(s):  
Enzymatic Activity ◽  
Ammonium Sulfate ◽  
High Efficiency ◽  
Specific Activity ◽  
Lipolytic Activity ◽  
Physical Adsorption ◽  
Lactobacillus Fermentum ◽  
Partial Purification ◽  
Bacterial Strains ◽  
Chitosan Beads

Background and Objectives: Due to the widespread use of lipase enzymes in various industries, finding native lipase pro- ducing microorganisms is of great value and importance. In this study, screening of lipase-producing lactobacilli from native dairy products was performed. Materials and Methods: Qualitative evaluation of lipolytic activity of lipase-producing lactobacilli was performed in differ- ent media containing olive oil. A clear zone observation around the colonies indicated the lipolytic activity. The strain with the highest enzymatic activity was identified. Determination of optimal pH and temperature of lipase activity was measured by spectrophotometry using p-nitrophenyl acetate (ρ-NPA) substrate. Partial purification of lipase enzyme was performed using 20-90% saturation ammonium sulfate. Eventually, lipase was immobilized by physical adsorption on chitosan beads. Results: Among screened lipolytic bacterial strains, one sample (5c isolate) which showed the highest enzymatic activity (5329.18 U/ml) was close to Lactobacillus fermentum. During characterization, the enzyme showed maximum activity in Tris-HCl buffer with pH 7, while remaining active over a temperature range of 5°C to 40°C. The results of the quantitative assay demonstrated that the fraction precipitated in ammonium sulfate at 20% saturation has the highest amount of lipolytic activity, with a specific activity of 22.0425 ± 3.6 U/mg. Purification folds and yields were calculated as 8.73 and 44%, respec- tively. Eventually, the enzyme was immobilized by physical adsorption on chitosan beads with a yield of 56.21%. Conclusion: The high efficiency of enzyme immobilization on chitosan beads indicates the suitability of this method for long-term storage of new lipase from native 5c isolate.

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