Enzymes Aspergillus niger

Studies of Aspergillus niger. Part XI. Enzymic Synthesis of a Pseudoaldobiuronic Acid, S. A. Barker, A. Gomez-Sanchez, and M. Stacey,/. Chem. Soc., (1959) 3264- 3269. 

Several reports regarding the directed evolution of enantioselective epoxide hydrolases (EHs) have appeared [23,57-59]. These enzymes constitute important catalysts in synthetic organic chemistry [4,60]. The first two reported studies concern the Aspergillus niger epoxide hydrolase (ANEH) [57,58]. Initial attempts were made to enhance the enantioselectivity of the AN E H -catalyzed hydrolytic kinetic resolution of glycidyl phenyl ether (rac-19). The WT leads to an Evalue of only 4.6 in favor of (S)-20 (see Scheme 2.4) [58]. 

Enzymes PPL, lipase from Pseudomonas fluorescens F-AP, lipase from Rhizopus orizae AP-6, lipase from Aspergillus niger, SP-254, lipase from Aspergillus oryzae P-2, Chirazyme WCPC, whole cell cultures of Penicillium citrinum WCPFL, whole cell cultures of Pseudomona fluorescens CAL-B, lipase from Candida antarctica B PS-C, lipase from Pseudomonas cepacia GCL, lipase from Geotrichum candidum. n.r. not reported. 

Table 2. Compilation of features and properties of Aspergillus niger pectin lyase genes and enzymes. WT, wild type n.d., not determined.

Endopolygalacturonases PGI and PGII isolated from a recombinant Aspergillus, niger and exopolygalacturonase (PGX) isolated from A. tubingensis are described elsewhere in this volume (see Benen et al. and Kester et al., respectively). For NMR spectroscopy the enzymes were lyophilized three times from DjO. 

Enzymic release of ferulic acid from sugar beet pulp using a specific esterase from Aspergillus niger... 

Source of Aspergillus niger strains, enzymes and substrates... 

SoKd substrate fermentation using agricultural wastes was considered to be used for the production of both enzymes in order to reduce the production costs. Production of glucoamylase from Aspergillus niger J8 was reported (1,3). This report concerned on the production of pectinases from Rhizopus sp. 26R in solid substrates composting of agricultural wastes, optimization of the conditions for pectinases production in solid substrates and the estimation of the production cost. 

Figure 9 Pectinases from Rhizopus sp. 26R showed high potential in enhancing the digestion of raw starch from ground cassava tuber when the enzymes were mixed with the glucoamylase of Aspergillus niger J8...

A novel nitrilase was purified from Aspergillus niger K10 cultivated on 2-cyanopyridine. It was found to be homologous to a putative nitrilase from Aspergillus fumigatus Af293. The nitrilase exhibited maximum activity at 45 °C and pH 8.0 with much less activity observed at slightly acid pH. Its substrate preference was for 4-cyanopyridine, benzonitrile, 1,4-dicyanobenzene, thio-phen-2-acetonitrile, 3-chlorobenzonitrile, 3-cyanopyridine, and 4-chlorobenzonitrile. ( )-2-Phenylpropionitrile was only poorly converted by this enzyme and with minimal enantioselectivity. The enzyme was shown to be multimeric (>650 kDa) and be stabilized in the presence of sorbitol and xylitol [57]. 

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