Catalytic Properties of Lipase Extracts from Aspergillus niger

Screening of lipolytic strains using Rhodamine-B/olive oil plate technique allowed the selection of Aspergillus niger MYA 135. Lipase production in submerged culture containing 2 % olive oil was enhanced by more than 50 % compared to basal cultural conditions. Optimal catalytic conditions for olive...

Full description

Bibliographic Details
Main Authors: Cintia M. Romero, Mario D. Baigori, Guillermo R. Castro, Licia M. Pera
Format: Article
Language:English
Published: University of Zagreb 2006-01-01
Series:Food Technology and Biotechnology
Subjects:
Online Access:http://hrcak.srce.hr/file/161925
id doaj-1cfaae3f6d444e4ebd727c295117fd8f
record_format Article
spelling doaj-1cfaae3f6d444e4ebd727c295117fd8f2020-11-25T01:40:44ZengUniversity of ZagrebFood Technology and Biotechnology1330-98621334-26062006-01-01442247252Catalytic Properties of Lipase Extracts from Aspergillus nigerCintia M. Romero0Mario D. Baigori1Guillermo R. Castro2Licia M. Pera3PROIMI, Av. Belgrano y Pasaje Caseros, 4000 Tucumán, ArgentinaPROIMI, Av. Belgrano y Pasaje Caseros, 4000 Tucumán, ArgentinaDepartment of Biomedical Engineering, Tufts University, Medford, MA 02155, USAPROIMI, Av. Belgrano y Pasaje Caseros, 4000 Tucumán, ArgentinaScreening of lipolytic strains using Rhodamine-B/olive oil plate technique allowed the selection of Aspergillus niger MYA 135. Lipase production in submerged culture containing 2 % olive oil was enhanced by more than 50 % compared to basal cultural conditions. Optimal catalytic conditions for olive oil-induced lipase were pH=6.5 and 30–35 °C. These values were shifted to the acid region (4.0–6.5) and 35–37 °C when lipase extract was produced under basal conditions. Slight changes of the residual lipase activity against the pH were found. However, preincubation at either 37 or 40 °C caused an increase in the olive oil-inducible lipolytic activity. On the contrary, lipase residual activity decreases in the 30–55 °C range when it was produced in basal medium. Lipolytic extracts were almost not deactivated in presence of 50 % water-miscible organic solvents. However, water-immiscible aliphatic solvents reduced the lipase activity between 20 and 80 %.http://hrcak.srce.hr/file/161925Aspergillus nigersubstrate specificitysolvent tolerancethermoresistanceenzyme stabilitylipase screening
collection DOAJ
language English
format Article
sources DOAJ
author Cintia M. Romero
Mario D. Baigori
Guillermo R. Castro
Licia M. Pera
spellingShingle Cintia M. Romero
Mario D. Baigori
Guillermo R. Castro
Licia M. Pera
Catalytic Properties of Lipase Extracts from Aspergillus niger
Food Technology and Biotechnology
Aspergillus niger
substrate specificity
solvent tolerance
thermoresistance
enzyme stability
lipase screening
author_facet Cintia M. Romero
Mario D. Baigori
Guillermo R. Castro
Licia M. Pera
author_sort Cintia M. Romero
title Catalytic Properties of Lipase Extracts from Aspergillus niger
title_short Catalytic Properties of Lipase Extracts from Aspergillus niger
title_full Catalytic Properties of Lipase Extracts from Aspergillus niger
title_fullStr Catalytic Properties of Lipase Extracts from Aspergillus niger
title_full_unstemmed Catalytic Properties of Lipase Extracts from Aspergillus niger
title_sort catalytic properties of lipase extracts from aspergillus niger
publisher University of Zagreb
series Food Technology and Biotechnology
issn 1330-9862
1334-2606
publishDate 2006-01-01
description Screening of lipolytic strains using Rhodamine-B/olive oil plate technique allowed the selection of Aspergillus niger MYA 135. Lipase production in submerged culture containing 2 % olive oil was enhanced by more than 50 % compared to basal cultural conditions. Optimal catalytic conditions for olive oil-induced lipase were pH=6.5 and 30–35 °C. These values were shifted to the acid region (4.0–6.5) and 35–37 °C when lipase extract was produced under basal conditions. Slight changes of the residual lipase activity against the pH were found. However, preincubation at either 37 or 40 °C caused an increase in the olive oil-inducible lipolytic activity. On the contrary, lipase residual activity decreases in the 30–55 °C range when it was produced in basal medium. Lipolytic extracts were almost not deactivated in presence of 50 % water-miscible organic solvents. However, water-immiscible aliphatic solvents reduced the lipase activity between 20 and 80 %.
topic Aspergillus niger
substrate specificity
solvent tolerance
thermoresistance
enzyme stability
lipase screening
url http://hrcak.srce.hr/file/161925
work_keys_str_mv AT cintiamromero catalyticpropertiesoflipaseextractsfromaspergillusniger
AT mariodbaigori catalyticpropertiesoflipaseextractsfromaspergillusniger
AT guillermorcastro catalyticpropertiesoflipaseextractsfromaspergillusniger
AT liciampera catalyticpropertiesoflipaseextractsfromaspergillusniger
_version_ 1725043738494894080