Extracellular lipolytic activity in <i>Phoma glomerata</i>

Several properties of the lipolytic activity exhibited by the conidial fungus <i>Phoma glomerata</i> were studied. Lipolytic activity in an aqueous buffer medium was measured on triacylglycerol, phosphoglyceride and cholesterol ester under different experimental conditions. The effect of...

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Detalles Bibliográficos
Autores principales: Pollero, Ricardo José, Gaspar, María Laura, Cabello, Marta Noemí
Formato: Articulo
Lenguaje:Inglés
Publicado: 2001
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/130944
Aporte de:
id I19-R120-10915-130944
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Naturales
Extracellular lipase
fungal esterase
lipolytic activity
microbial enzyme
non-specific esterase
Phoma glomerata
phospholipid hydrolysis
sterol ester degradation
triolein degradation
spellingShingle Ciencias Naturales
Extracellular lipase
fungal esterase
lipolytic activity
microbial enzyme
non-specific esterase
Phoma glomerata
phospholipid hydrolysis
sterol ester degradation
triolein degradation
Pollero, Ricardo José
Gaspar, María Laura
Cabello, Marta Noemí
Extracellular lipolytic activity in <i>Phoma glomerata</i>
topic_facet Ciencias Naturales
Extracellular lipase
fungal esterase
lipolytic activity
microbial enzyme
non-specific esterase
Phoma glomerata
phospholipid hydrolysis
sterol ester degradation
triolein degradation
description Several properties of the lipolytic activity exhibited by the conidial fungus <i>Phoma glomerata</i> were studied. Lipolytic activity in an aqueous buffer medium was measured on triacylglycerol, phosphoglyceride and cholesterol ester under different experimental conditions. The effect of storage temperature on the stability of the hydrolytic activity, and optimal conditions of temperature and time of maximal activity were determined. The optimal conditions for maximal lipolytic activity were found to be 40–50 °C and 1 h. The activity released to the medium by 1 mg cells for 1 h at 40 °C was stated as the enzyme released unit (ERU). The protein fraction of MW > 50 kDa obtained by ultrafiltration of the medium, was active on the three substrates assayed, and it showed a non-specific hydrolytic activity on both the 1- and 2-acyl esters either in the neutral glyceride or in the phosphoglyceride. A protein of M<sub>r</sub> approx. 75 kDa was the only one that showed esterase activity. The crude medium, stored at −15 °C, maintained its initial hydrolytic activity on triacylglycerol for at least 42 days, though when it was kept for 10 days at 4 °C, the activity fell to 50%. Kinetic parameters using substrates such as triolein (TO), dipalmitoyl phosphatidylcholine (DPPC) and cholesteryl oleate (ChoO), were comparatively evaluated. The activity of the enzyme in the hydrolysis of TO showed the highest values, whereas the maximal specific activities were less when the enzyme was assayed against DPPC and ChoO.
format Articulo
Articulo
author Pollero, Ricardo José
Gaspar, María Laura
Cabello, Marta Noemí
author_facet Pollero, Ricardo José
Gaspar, María Laura
Cabello, Marta Noemí
author_sort Pollero, Ricardo José
title Extracellular lipolytic activity in <i>Phoma glomerata</i>
title_short Extracellular lipolytic activity in <i>Phoma glomerata</i>
title_full Extracellular lipolytic activity in <i>Phoma glomerata</i>
title_fullStr Extracellular lipolytic activity in <i>Phoma glomerata</i>
title_full_unstemmed Extracellular lipolytic activity in <i>Phoma glomerata</i>
title_sort extracellular lipolytic activity in <i>phoma glomerata</i>
publishDate 2001
url http://sedici.unlp.edu.ar/handle/10915/130944
work_keys_str_mv AT polleroricardojose extracellularlipolyticactivityiniphomaglomeratai
AT gasparmarialaura extracellularlipolyticactivityiniphomaglomeratai
AT cabellomartanoemi extracellularlipolyticactivityiniphomaglomeratai
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