A Study of the Esterases and Their Function in Candida lipolytica, Aspergillus niger and a Yeast-like Fungus

Lloyd, G.I.; Morris, E. O.; Smith, John E.

doi:10.1099/00221287-63-2-141

Cited by 26 publications

(6 citation statements)

References 14 publications

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“…Lipases from yeasts are gaining industrial interest with applications in laundry detergents and in dairy industries (Burden and Eveleight 1990), while little attention has so far been paid to esterases from yeasts (Lloyd et al 1971;Basaran and Hang 2000). Apparently, in the present study, the occurrence of EsA was essentially associated with basidiomycetes, while the occurrence of LipA was associated with ascomycetes (Tables 1 and 2).…”

Section: Discussionmentioning

confidence: 46%

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Extracellular enzymatic activity profiles in yeast and yeast-like strains isolated from tropical environments

2002

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Aims: The objective of this study was to investigate the extracellular enzymatic activity (EEA) profile of yeasts isolated from tropical environments of the Brazilian rain forest. This screening survey could constitute the first approach in selecting yeast strains of environmental origin potentially exploitable as enzyme producers. Methods and Results: In this study, 348 yeast (193 ascomycetes and 155 basidiomycetes) and 46 yeast-like strains (Aureobasidium pullulans) were screened for their EEA profile. The spread occurrence of extracellular amylases, esterases, lipases, proteases, pectinases and chitinases appeared to be a strain-related character. Conclusions: Yeasts isolated from tropical environments could represent a promising source of EEA. Selected strains showed maximum levels of EEA under acidic or neutral conditions. Significance and Impact of the Study: This study demonstrated the potential for yeasts isolated from extreme environments as sources of industrially relevant enzymes for biotechnological purposes.

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Section: Discussionmentioning

confidence: 46%

Section: Discussionmentioning

confidence: 99%

Extracellular enzymatic activity profiles in yeast and yeast-like strains isolated from tropical environments

2002

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“…Most of the microbial esterases are usually considered as inducible enzymes, their production being promoted by their substrates (Donaghy and Mckay 1992;Isobe and Wakao 1996;Lloyd et al 1971). When Tween 80 was omitted from the growth medium, the lipolytic activity from strain DF-E4 could still be detected from fractions E, I and M, indicating that the extracellular esterase is constitutively produced irrespective of the presence of inducer (Tween 80).…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of a novel extracellular carboxylesterase from the moderately halophilic bacterium Thalassobacillus sp. strain DF-E4

Guo

Song

et al. 2010

Ann Microbiol

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An extracellular carboxylesterase from the moderately halophile Thalassobacillus sp. strain DF-E4 was purified to 8-fold with 11% recovery and specific activity of 2,046 U mg −1 . The molecular mass of the native enzyme was approximately 49 kDa as determined by analytical ultracentrifugation, while SDS-PAGE analysis showed a single protein band corresponding to a molecular mass of 45 kDa, suggesting that the enzyme was a monomer. Among the pNP (p-nitrophenyl) esters tested, p-nitrophenyl butyrate (C 4 ) was hydrolyzed most effectively, with K m and V max values of 0.69 mM and 0.84 μmol min −1 mg −1 , respectively, and the optimum activity occurred at pH 8.5, 40°C and 0.5 M NaCl (w/v). The enzyme activity appeared to be stable over pH 6.0-9.5 and up to 45°C for 1 h. Tests of substrate specificity and inhibitor susceptibility revealed it was a serine-type carboxylesterase (EC 3.1.1.1), rather than a lipase. None of the divalent cations tested enhanced the enzyme activity, while most of them had no effect or slightly inhibited the activity. The enzyme activity was strongly inhibited by PMSF, PAO and DEPC, implying that serine, cysteine and histidine residues at the active site were essential for catalysis.

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“…Apparently, most cells, whether mammalian cells, yeasts cells, or gram-positive or gram-negative bacteria, can hydrolyze FDA or cFDA (2,5,21,24). A number of studies on the esterase activity of yeast cells (10,17,18,31,33), which indicated that several different activities are present in S. cerevisiae, have been carried out. However, generally, p-nitrophenyl acetate or naphthyl acetates were used as esterase substrates, and there is no available information about FDA or cFDA conversion by intracellular esterases in yeast cells.…”

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confidence: 99%

Characterization of uptake and hydrolysis of fluorescein diacetate and carboxyfluorescein diacetate by intracellular esterases in Saccharomyces cerevisiae, which result in accumulation of fluorescent product

Breeuwer

Drocourt

Bunschoten

et al. 1995

Appl Environ Microbiol

216

112

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Flow cytometry is a rapid and sensitive method which may be used for the detection of microorganisms in foods and drinks. A key requirement for this method is a sufficient fluorescence staining of the target cells. The mechanism of staining of the yeast Saccharomyces cerevisiae by fluorescein diacetate (FDA) and 5-(and 6-)carboxyfluorescein diacetate (cFDA) was studied in detail. The uptake rate of the prefluorochromes increased in direct proportion to the concentration and was not saturable, which suggests that transport occurs via a passive diffusion process. The permeability coefficient for cFDA was 1.3 ؋ 10 ؊8 m s ؊1 . Once inside the cell, the esters were hydrolyzed by intracellular esterases and their fluorescent products accumulated. FDA hydrolysis (at 40؇C) in cell extracts could be described by first-order reaction kinetics, and a rate constant (K) of 0.33 s ؊1 was calculated. Hydrolysis of cFDA (at 40؇C) in cell extracts was described by Michaelis-Menten kinetics with an apparent V max and K m of 12.3 nmol ⅐ min ؊1 ⅐ mg of protein ؊1 and 0.29 mM, respectively. Accumulation of fluorescein was most likely limited by the esterase activity, since transport of FDA was faster than the hydrolysis rate. In contrast, accumulation of carboxyfluorescein was limited by the much slower transport of cFDA through the cell envelope. A simple mathematical model was developed to describe the fluorescence staining. The implications for optimal staining of yeast cells with FDA and cFDA are discussed.

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A Study of the Esterases and Their Function in Candida lipolytica, Aspergillus niger and a Yeast-like Fungus

Cited by 26 publications

References 14 publications

Extracellular enzymatic activity profiles in yeast and yeast-like strains isolated from tropical environments

Extracellular enzymatic activity profiles in yeast and yeast-like strains isolated from tropical environments

Purification and characterization of a novel extracellular carboxylesterase from the moderately halophilic bacterium Thalassobacillus sp. strain DF-E4

Characterization of uptake and hydrolysis of fluorescein diacetate and carboxyfluorescein diacetate by intracellular esterases in Saccharomyces cerevisiae, which result in accumulation of fluorescent product

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