Rhizopus niger

I la -Hydroxy-3,20-dioxo-pregnen-(4) Rhizopus riigrians ATCC 6227b4 24°/, Aspergillus niger ... 

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. 

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. 

The efficiency in raw cassava starch hydrolyzation of pectinases from Rhizopus sp. 26R compared with a commercial pectinase when mixed with Glucoamylase from Aspergillus niger J8. 

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...

Alternaria sp Aspergillus niger Cladosporium herbarum Colletotrichum gossypii Fusarium sp Rhizopus stolonifer... 

Figure 7.10 Schematic representation of the domain structure of glucoamylases Aspergillus niger glucoamylase-1, with starch-binding, linker and catalytic domains Aspergillus mger glucoarriylase-2, with only the catalytic domain Rhizopus nievus glucoamylase-l, with starch binding, linker and catalytic domains...

These transformations indicated that the starch binding domain of Rhizopus sp. glucoamylase was located at the N-terminus, and attached to the catalytic domain by a small linker domain (Figure 7.10). This is in contrast with the A. niger glucoamy-lases that have an opposite structure, with the catalytic domain at the N-terminus and the starch binding domain at the C-terminus. 

Lipases can be classified into groups that reflect their specificity. The common lipases include non-specific lipases that do not discriminate between the position or the type of the fatty acid on the triacylglycerol (e.g., lipase from Candida cylindracea) and 1,3-specific lipases that act only at the sn-l and sn-3 positions of the triacylglycerol (e.g., lipases from Aspergillus niger and Rhizopus species). In addition, some lipases are specific for a specific fatty acid type (e.g., lipase from Geotrichum candidum). 

Pectinaseb carbohydrase (1) Aspergillus niger war. (2) Rhizopus oryzae var. (1) poly(l,4-a-D-galacturonide) glycanohydrolase (2) pectin pectylhydrolase (3) poly(l,4-a-D-glacturonide) lyase (4) poly(methoxyl-L- galacturonide) lyase 3.2.1.15 3.1.1.11 4.2.2.2 4.2.2.10... 

Application and Principle This procedure is used to determine the a-amylase activity of enzyme preparations derived from Aspergillus niger var. Aspergillus oryzae var. Rhizopus oryzae var. and barley malt. The assay is based on the time required to obtain a standard degree of hydrolysis of a starch solution at 30° 0.1°. The degree of hydrolysis is determined by comparing the iodine color of the hydrolysate with that of a standard. 

Aspergilllus niger Rhizopus arrhizus Mucor miehei Candida antarctica A Penicillium expan sum... 

The Aspergillus niger enzyme contained o-mannose, D-glucose, and D-galactose, whereas that from Rhizopus delemar contained D-mannose and 2-amino-2-deoxy-D-glucose. 

Much work has been published on the microbiological reduction of a,p-unsaturated ketones. Under anaerobic conditions the reduction of A -3-keto steroids by Clostridium paraputrificum led to the 3-keto 5p-derivatives (Scheme 69) Similar transformations were observed previously with Bacillus putrifi-cus, Penicillium decumbens Rhizopus nigricans or Aspergillus niger. In most cases further reduction led to the corresponding 3a-hydroxy 5P-derivatives. 

Interesterification can also be catalysed by enzymes, many of which show useful specificities. The 1,3-specific lipases, such as those derived from Aspergillus niger, Mucor javanicus, M. miehei, Rhizopus arrhizus, R. delemar, and R. niveus, are particularly useful for interesterification. They are used to effect acyl exchange at the sn- and 3 positions while leaving acyl groups at the sn-2 position unchanged. 

Lipases that are in-1,3 specific include those from Mucor miehei, Mucor java-nicus, Aspergillus niger. Pseudomonas fluorescens, Rhizopus delemar, Rhizopus arrhizus, and pancreatic lipase (11, 25-27). These enzymes cleave the fatty acids only from the sn-l and sn-3 positions of the glycerol backbone of TAGs. Thus, with these lipases, TAGs are hydrolyzed to afford FFA, 1,2 (2,3)-DAGs and 2-MAGs. 

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