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...
Main Authors: | , , , |
---|---|
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 |