Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources

Pavezzi, Fabiana Carina; Gomes, Eleni; Silva, Roberto da

doi:10.1590/s1517-83822008000100024

Cited by 39 publications

(24 citation statements)

References 35 publications

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“…Glucoamylase activity increased from day 3 to day 5 and from day 11 to day 12, with maximum levels of glucoamylase activity obtained at day five (5) and day twelve (12) of submerged fermentation. Similar observations were reported by Fabiana et al [18], in their report; the maximum glucoamylase activity was achieved on day 3 of the submerged fermentation. Also, the decrease in glucoamylase production from day 6 to day 10 and from day 12 to day 14 could be attributed to high glucose concentration obtained by the microorganism, Christiane et al [19], in their research, reported that glucoamylase production by Aspergillus niger is repressed due to high glucose concentration in the microorganism, nevertheless, when glucose concentration decreases in the microorganism, the microorganism ( Aspergillus niger) then starts to produce glucoamylase again, to hydrolyze the substrate (in this case, amylopectin from guinea corn starch) to produce more glucose due to increased production of glucoamylase, as observed from the peaks obtained.…”

Section: Amylopectin Yieldsupporting

confidence: 91%

Effect of Divalent Metal Ions on Glucoamylase Activity of Glucoamylase Isolated from Aspergillus niger

Pc¹,

Ku²,

Ezugwu³

et al. 2016

Ferment Technol

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This study investigates the production of glucoamylase from Aspergillus niger in a submerged fermentation process using amylopectin fractionated from guinea corn starch as the carbon source. This work also studies the effect of a few metal ions (Ca 2+ , Zn 2+ , Co 2+ , Fe 2+ , Mn 2+ and Pb 2+ ) concentration on the glucoamylase activity. A Fourteen day experimental study was carried out to determine the day of highest glucoamylase activity. Maximum glucoamylase activity was observed on day five of the submerged fermentation; hence, day five was mass produced. The specific activity for the crude enzyme was found to be 729.45 U/mg. The crude enzyme was purified to the level of gel filtration (using sephadex G-100) via ammonium sulphate precipitation. Ammonium sulphate saturation of 70% was found suitable to precipitate the enzyme. After ammonium sulphate precipitation and gel filtration, the specific activities were found to be 65.98 U/mg and 180.52 U/mg respectively. The glucoamylase activity was enhanced by 2 mM to 5 mM of Ca 2+ , Co 2+ , Fe 2+ , Mn 2+ and Zn 2+ but Pb 2+ had inhibitory effect on the enzyme. The Michaelis constant, Km and maximum velocity Vmax of the enzyme was obtained from the Lineweaver-Burk plot of initial velocity data at different substrate concentrations. They were found to be 770.75 mg/ml and 2500 µmol/min respectively, when using cassava starch as substrate. The enzyme glucoamylase is known to have useful applications in food processing industries and fermentation biotechnology.

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Section: Amylopectin Yieldsupporting

confidence: 91%

Effect of Divalent Metal Ions on Glucoamylase Activity of Glucoamylase Isolated from Aspergillus niger

Pc¹,

Ku²,

Ezugwu³

et al. 2016

Ferment Technol

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“…at pH varying between 5 and 6. In contrast [19] reported pH 3.5 and pH 4.0 to be the best for the production of α-amylase by B. amylolique faciens and A.…”

Section: -Effect Of Phmentioning

confidence: 86%

Manufacture Enzyme From the Fungus A. Flavus

Mezeal¹

2017

WJPR

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Amylases are enzymes which hydrolyze the starch molecules into polymers composed of glucose units, Amylases are among the most important enzymes and are of great significance for biotechnology, They can be obtained from several sources, such as plants, animals and microorganisms. Amylases have potential application in a wide number of industrial processes such as food, fermentation, textile paper, detergent, and pharmaceutical industries. The effect of temperature on amylase activity A. flavus H4 was studied by varying the temperature from 20°C to 40°C. It is clear from the results that a temperature of 28°C was found to be best suitable for amylase activity and maximum activity found was 8.7U\ml, it was observed that at 20°C enzyme activities were low 4.5 U\ml and showed a gradual increase with the increase in temperature to 28°C. Further increase in temperature resulted in decrease in production of amylase that at 42°C enzyme activities were 4.5U\ml. The effect of pH on amylase activity of A. flavus was studied by varying pH from 4.5 to7.5, Under experimental conditions, a maximum enzyme activity was produced at pH 5.5, 7.1U/ml and the lowest at pH 7.5, 5.2U/ml. The cultures were incubated for 2 -8 days, The enzyme was extracted and the specific activity of the amylase produced at different days of incubation was 4.1 U/ml in 2 days of incubation and The specific activity was 7.2 U/ml for the enzyme at 6 days of incubation, while The specific activity was 6.8 U/ml for the enzyme at 8 days of incubation.

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“…In lignocellulolytic waste there were traces of starch, on which amylase acted and produced glucose monomers. Glucoamylase consecutively hydrolyzes α-1,4 glycosidic bonds from non-reducing ends of starch, resulting in the production of glucose (Pavezzi et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Enzyme profiling of lignocellulolytic fungi

Acharya¹,

Chabhadiya²,

Shah³

et al. 2010

International Journal of Biological and Chemical Sciences

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Lignocellulolytic fungi produce a variety of lignocellulolytic enzymes which are responsible for the biodegradation of lignocellulosic agro-wastes in nature. These enzymes are also useful for biofuel production, bio-bleaching, bio-pulping etc. We have isolated ecodiversely different seventeen fungi from ecorich soils of Gandhinagar region, Gujarat, India. The objective of this work was to study enzyme production profile by lignocellulolytic fungi, using wheat straw as a model agro-waste by solid state fermentation. Most of these lignocellulolytic fungi have been found to express enzyme activities like filter paper activity (FPase), endoglucanase, exocellulase, β-glucosidase, xylanase, glucoamylase, manganese peroxidase (MnP) and protease. Among these, A. niger, A. oryzae and Sporotrichum sp. produce endocellulase and xylanase in significant amount. A. niger and Sporotrichum sp. gave 52.47 U/g and 69.441 U/g endocellulase activity, and 48.107 U/g and 112.649 U/g xylanase activity, respectively.

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Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources

Cited by 39 publications

References 35 publications

Effect of Divalent Metal Ions on Glucoamylase Activity of Glucoamylase Isolated from Aspergillus niger

Effect of Divalent Metal Ions on Glucoamylase Activity of Glucoamylase Isolated from Aspergillus niger

Manufacture Enzyme From the Fungus A. Flavus

Enzyme profiling of lignocellulolytic fungi

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