Growth and hydrolase profiles can be used as characteristics to distinguish Aspergillus niger and other black aspergilli

被引:53
作者
Meijer, M. [1 ,2 ]
Houbraken, J. A. M. P. [2 ]
Dalhuijsen, S. [1 ]
Samson, R. A. [2 ]
de Vries, R. P. [1 ,2 ]
机构
[1] Univ Utrecht, NL-3584 CH Utrecht, Netherlands
[2] CBS KNAW, Fungal Biodivers Ctr, NL-3584 CT Utrecht, Netherlands
关键词
ALPHA-GALACTOSIDASE; BETA-GALACTOSIDASE; DEGRADING ENZYMES; CELL-WALL; PURIFICATION; GENES; DEGRADATION; CARBONARIUS; XYLOSIDASE; ACULEATUS;
D O I
10.3114/sim.2011.69.02
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Wild type Aspergillus niger isolates from different biotopes from all over the world were compared to each other and to the type strains of other black Aspergillus species with respect to growth and extracellular enzyme profiles. The origin of the A. niger isolate did not result in differences in growth profile with respect to monomeric or polymeric carbon sources. Differences were observed in the growth rate of the A. niger isolates, but these were observed on all carbon sources and not specific for a particular carbon source. In contrast, carbon source specific differences were observed between the different species. Aspergillus brasiliensis is the only species able to grow on D-galactose, and A. aculeatus had significantly better growth on Locus Bean gum than the other species. Only small differences were found in the extracellular enzyme profile of the A. niger isolates during growth on wheat bran, while large differences were observed in the profiles of the different black aspergilli. In addition, differences were observed in temperature profiles between the black Aspergillus species, but not between the A. niger isolates, demonstrating no isolate-specific adaptations to the environment. These data indicate that the local environment does not result in stable adaptations of A. niger with respect to growth profile or enzyme production, but that the potential is maintained irrespective of the environmental parameters. It also demonstrates that growth, extracellular protein and temperature profiles can be used for species identification within the group of black aspergilli.
引用
收藏
页码:19 / 30
页数:12
相关论文
共 29 条
[1]   Multiple α-galactosidases from Aspergillus niger:: purification, characterization and substrate specificities [J].
Ademark, P ;
Larsson, M ;
Tjerneld, F ;
Stålbrand, H .
ENZYME AND MICROBIAL TECHNOLOGY, 2001, 29 (6-7) :441-448
[2]   Cloning and characterization of Aspergillus niger genes encoding an α-galactosidase and a β-mannosidase involved in galactomannan degradation [J].
Ademark, P ;
de Vries, RP ;
Hägglund, P ;
Stålbrand, H ;
Visser, J .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (10) :2982-2990
[3]   Aspergillus niger genomics: Past, present and into the future [J].
Baker, Scott E. .
MEDICAL MYCOLOGY, 2006, 44 :S17-S21
[4]   Study on heterogeneity of β-glucosidase from Aspergillus species by using counter-current distribution [J].
Brumbauer, A ;
Johansson, G ;
Réczey, K .
JOURNAL OF CHROMATOGRAPHY B, 2000, 743 (1-2) :247-254
[5]   Aspergillus vadensis, a new species of the group of black Aspergilli [J].
de Vries, RP ;
Frisvad, JC ;
van de Vondervoort, PJI ;
Burgers, K ;
Kuijpers, AFA ;
Samson, RA ;
Visser, J .
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY, 2005, 87 (03) :195-203
[6]   A new black Aspergillus species, A. vadensis, is a promising host for homologous and heterologous protein production [J].
de Vries, RP ;
Burgers, K ;
van de Vondervoort, PJI ;
Frisvad, JC ;
Samson, RA ;
Visser, J .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2004, 70 (07) :3954-3959
[7]   Regulation of Aspergillus genes encoding plant cell wall polysaccharide-degrading enzymes;: relevance for industrial production [J].
de Vries, RP .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2003, 61 (01) :10-20
[8]   Aspergillus enzymes involved in degradation of plant cell wall polysaccharides [J].
de Vries, RP ;
Visser, J .
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2001, 65 (04) :497-+
[9]   β-glucosidases from five black Aspergillus species:: Study of their physico-chemical and biocatalytic properties [J].
Decker, CH ;
Visser, J ;
Schreier, P .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2000, 48 (10) :4929-4936
[10]   Production, partial purification and some properties of β-galactosidase from Aspergillus carbonarius [J].
El-Gindy, A .
FOLIA MICROBIOLOGICA, 2003, 48 (05) :581-584