scholarly journals The effects of Psidium guajava leaf extract on the production of cellulases and glucose oxidases by Aspergillus niger

2020 ◽  
Vol 5 (2) ◽  
pp. 118-122
Author(s):  
Isheanesu Dzambi ◽  
Rumbidzai Mangoyi

Aspergillus niger, is a filamentous fungus and producer of industrial enzymes such as glucose oxidases and cellulases. These enzymes are naturally produced by the fungus in order to digest and absorb nutrients from its environment. However, the enzyme quantities that are naturally produced are low. Thus, the aim of this study was to determine the effects of Psidum guajava leaf extract on the production of cellulases and glucose oxidases from Aspergillus niger. The leaves of Psidium guajava were extracted using absolute methanol. Aspergillus niger was then grown in the presence and absence of the extract in order to investigate the effects of extract on enzyme production by the fungus. The enzymes secreted into the broth medium were isolated by centrifugation. The supernatant which contained the secreted enzymes was used for the determination of enzyme activity. Enzyme activity was determined using the specific substrate for the specific enzyme, such as 2 % cellulose for cellulase and standard glucose solution for glucose oxidase. The results showed that the Psidium guajava leaf extract had an effect on production and activity of cellulases and glucose oxidases. From this study, it was noted that the Psidium guajava leaf extract may be used to induce the production of enzymes by Aspergillus niger and these enzymes may be of industrial use.

2019 ◽  
Vol 9 (1) ◽  
pp. 41-45
Author(s):  
Tafadzwa Zharare ◽  
Rumbidzai Mangoyi

The use of enzymes on industrial scale saves a lot of energy and avoids pollution, thus holding a promise for green and economically sustainable alternative strategies in industrial transformations.  Generally, the fungi Aspergillus niger secretes enzymes which can be used in different industries. Thus, coming up with these enzymes in large amounts will definitely result in reduced costs encountered in importing them for industrial use.  This study focussed on isolation and activity determination of an enzyme phosphatase secreted by Aspergillus niger.  This enzyme can be of great importance in molecular biology industries, particularly for recombinant DNA technology.  For this study, pure cultures of Aspergillus niger were used.  Aspergillus niger was resuscitated on potato dextrose agar and then subcultured in Adam’s medium, a medium specific for the production of phosphatase.  Cells were centrifuged and the filtrate was collected whilst the residue was discarded. The filtrate was expected to contain the crude enzyme phosphatase since Aspergillus niger secretes the extracellular enzyme into the medium. Disodium phenyl phosphate was used as a substrate for the determination of the phosphatase activity. The enzyme activity was determined spectrophotometrically by reading absorbance of phenol formed in the presence of enzyme and the substrate. The concentration of phenol liberated was then used to calculate the enzyme activity expressed in King Armstrong Units (KAU).  Further work on enzyme activity determination was done by varying enzyme and substrate concentrations.  Results showed that the isolated alkaline phosphatase had activity of 4.0 KAU and 4.5 KAU at 25 ºC and 37 ºC respectively. Acidic phosphatase had activity of 5 KAU and 7 KAU at 25 ºC and 37 ºC respectively. Rate of activity increased upon increasing enzyme concentration and substrate.  Thus, Aspergillus niger produces the enzyme phosphatase, however, there is need to induce the production of these enzymes for industrial use.


2019 ◽  
Vol 2 (1) ◽  
pp. 67-74
Author(s):  
Oleen Machona ◽  
Ronald Mlambo ◽  
Tafadzwa Zharare ◽  
Rumbidzai Mangoyi

2019 ◽  
Vol 37 (1) ◽  
pp. 116
Author(s):  
Chenliang FAN ◽  
Yuhong ZHANG ◽  
Chuan WANG ◽  
Zhenlei PENG ◽  
Zhirong GAO

2021 ◽  
Author(s):  
Syarifah Ramadhani Lubis ◽  
Subandi Subandi ◽  
Muntholib Muntholib ◽  
Jamilah Abbas ◽  
Tjandrawati Mozef

1966 ◽  
Vol 12 (5) ◽  
pp. 308-313 ◽  
Author(s):  
Albert W Opher ◽  
Charles S Collier ◽  
Joseph M Miller

Abstract A convenient electrophoretic procedure for the separation and quantitation of lactate dehydrogenase (LDH) isoenzymes is described. The system uses polyacetate Sepraphore III strips.* The areas of activity are shown by incubation with an LDH substrate combined with tetra-nitro-blue-tetrazolium. The reduction of the latter to the purple formazan is quantitatively related to the enzyme activity. Quantitative determination of the individual colored areas is performed by densitometry.


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