Production of an esterase from Fusarium oxysporum catalysing transesterification reactions in organic solvents

Christakopoulos, Paul; Tzalas, B.; Mamma, Diomi; Stamatis, Haralambos; Liadakis, G.; Tzia, Constantina; Kekos, Dimitris; Kolisis, Fragiskos N.; Macris, Basil J.

doi:10.1016/s0032-9592(98)00039-9

Cited by 13 publications

(5 citation statements)

References 21 publications

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“…These results enhance its utility at different area for which thermal stability at high temperature is not required. Similar temperature optima were reported for Fusarium oxysporum esterase which plays a significant role in producing flavoring and fragrance compounds from geraniol and fatty acids (Karra-Chaabouni et al 1996;Christakopoulos et al 1998), L. casei CL96 esterase and lipase hydrolyze milk fat for the purpose of flavor enhancement in the manufacture of cheese-related products (Choi and Lee 2001), and Bacillus coagulans esterase catalyzes the enantioselective hydrolysis of the racemic ester of 1,2-O-isopropylidene glycerol, a bioactive molecule (Molinari et al 1996).…”

Section: Esterase From Lycoperdon Perlatumsupporting

confidence: 61%

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

Çolak

Camedan

Faiz

et al. 2009

Journal of Food Biochemistry

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Lycoperdon perlatum Pers. (Lycoperdaceae, Agaricales, Agaricomycetidae, Agaricomycetes, Basidiomycota, Fungi) was evaluated for its esterolytic potential. Native electrophoresis of the crude extracts showed four bands having Rf values of 0.34, 0.39, 0.52 and 0.59. The esterase showed the highest activity toward a short‐chain substrate, p‐nitrophenyl acetate. Optimum reaction conditions for L. perlatum crude extract were attained at pH 8.0 and 40C. Esterolytic activity of enzyme extract was stimulated in the presence of Mn2+, Fe2+, Ca2+ and Zn2+ in the reaction mixture. The enzyme activity was stimulated by incubation at pH 6.0 but retained 77% of its original activity at its optimum pH after 24 h. Thermal inactivation was displayed after incubation for 20 min at various temperatures above 30C. At 1 mM final concentration, 2‐mercaptoethanol, dithiothreitol, ethylenediamine tetraacetic acid and p‐methylphenyl sulfonylfluoride inhibited the esterolytic reaction. These results support that the crude L. perlatum extract possesses an esterolytic activity having properties similar to other esterases. PRACTICAL APPLICATIONS Esterases catalyzing the cleavage and formation of ester bonds are known α/β‐hydrolases (EC 3.1.1.X). Esterases are used for the synthesis of flavor esters for the food industry, modification of triglycerides for fat and oil industry and resolution of racemic mixtures used for the synthesis of fine chemicals for the pharmaceutical industry. Therefore, the search for new enzyme sources is important for the development of new enzymes and applications.

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Section: Esterase From Lycoperdon Perlatumsupporting

confidence: 61%

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

Çolak

Camedan

Faiz

et al. 2009

Journal of Food Biochemistry

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“…These results were in agreement with those obtained using CCD, and were considered by the authors as a validation of the optimal composition of the growth medium used in this study. Similar data were obtained by Christakopoulos et al [5], in a study about the production of esterase by F. oxysporum. Under optimal conditions, these authors reported a yield of 7.3 U/mL in a liquid growth medium and 19.4 U/g in a solid medium.…”

Section: Experimental Design For Medium Composition Optimizationsupporting

confidence: 90%

Cutinase production by Fusarium oxysporum in liquid medium using central composite design

Pio

Macêdo

2007

J Ind Microbiol Biotechnol

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The objective of the present study was to measure the production of cutinase by Fusarium oxysporum in the presence of several carbon and nitrogen sources (glycides, fatty acids and oils, and several organic and inorganic nitrogen sources), trying to find a cost-effective substitute for cutin in the culture medium as an inducer of cutinase production. The results were evaluated by the Tukey test, and flaxseed oil was found to give the best results as a cutinase inducer. The authors optimized the composition of the growth medium employing response surface methodology. The experimental results were fitted to a second-order polynomial model at a 95% level of significance (p < 0.05). The greatest cutinolytic activity was obtained in a liquid mineral medium supplemented with flaxseed oil, showing an increase in enzymatic activity from 11 to 22.68 U/mL after 48 h of fermentation. A CCD study of the fermentation conditions was carried out, and the best production of cutinase was registered with the use of 30 degrees C and 100 rpm. These results support the use of flaxseed oil as a substitute for cutin, which is difficult and expensive to obtain, for the production of cutinase in a larger scale.

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“…Igualmente, no se podría concluir con base en los resultados que este tipo de enzimas no son expresadas por los hongos de este género, ya que diferentes autores han reportado la expresión de enzimas lipolíticas en el género Fusarium (14,(27)(28)(29). Christakopoulos et al, 1998, reportaron la producción de una esterasa por Fusarium oxysporum y encuentran que cuando se usa como sustrato p-nitrofenil-laurato y p-nitrofenil-palmitato, la actividad de la enzima es nula (30), lo que no ocurre cuando se usa p-nitrofenil-butirato y p-nitrofenil-acetato con mayor actividad para el p-nitrofenilbutirato. Este resultado sugiere que el uso de ésteres de cadena larga limita la actividad enzimática, o en su defecto la expresión de la enzima, y ello impide la determinación de enzimas lipolíticas (11,30).…”

Section: Actividad Lipolíticaunclassified

“…Christakopoulos et al, 1998, reportaron la producción de una esterasa por Fusarium oxysporum y encuentran que cuando se usa como sustrato p-nitrofenil-laurato y p-nitrofenil-palmitato, la actividad de la enzima es nula (30), lo que no ocurre cuando se usa p-nitrofenil-butirato y p-nitrofenil-acetato con mayor actividad para el p-nitrofenilbutirato. Este resultado sugiere que el uso de ésteres de cadena larga limita la actividad enzimática, o en su defecto la expresión de la enzima, y ello impide la determinación de enzimas lipolíticas (11,30). Lo anterior pudo ocasionar la no determinación de lipasas en las pruebas de actividad enzimática, ya que se usó p-nitrofenil-palmitato (éster de cadena larga), como sustrato de reacción (31).…”

Section: Actividad Lipolíticaunclassified

Evaluación de actividades enzimáticas de Fusarium spp., aislados de lesiones en humanos, animales y plantas

et al. 2011

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Objective. To determine amylolytic, cellulolytic, lipolytic, pectinolytic and proteolytic activities in 32 Fusarium spp. isolates from humans, animals and plants. Materials and methods. Qualitative determination of enzymatic activities was done by measuring hydrolysis halos in agar plates with their corresponding substrate. Quantitative determination was done by colorimetric techniques, using liquid culture supernatants to determine the respective substrate degradation. Results. All isolates showed enzymatic activities from a qualitative point of view, except amylolytic and lipolytic. Quantitative determination was possible for all the evaluated enzymes except lipases. Conclusion. The determination of amylolytic, cellulolytic, pectinolytic and proteolytic enzymatic profiles of each of the Fusarium isolates assessed suggests their capacity to degrade these substrates, irrespectively of their origin. Key words: Fusarium, multihost pathogen, amylases, celluloses, pectinases, proteases, lipases

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Production of an esterase from Fusarium oxysporum catalysing transesterification reactions in organic solvents

Cited by 13 publications

References 21 publications

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM,LYCOPERDON PERLATUM

Cutinase production by Fusarium oxysporum in liquid medium using central composite design

Evaluación de actividades enzimáticas de Fusarium spp., aislados de lesiones en humanos, animales y plantas

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