Recombinant Glucoamylase Production byAspergillus nigerB1 in Chemostat and pH Auxostat Cultures

Swift, Richard J.; Wiebe, Marilyn G.; Robson, Geoffrey D.; Trinci, Anthony P. J.

doi:10.1006/fgbi.1998.1089

Cited by 39 publications

(37 citation statements)

References 35 publications

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“…glucoamylases from Aspergillus and Rhizopus strains which are described as susceptible to denaturation at temperatures above 60ºC (9,20). The enzymes were similar to glucoamylases from thermophilic fungi such as Talaromyces duponte, Thermomyces lanuginosus and H. grisea that have optima at 75, 70 and 60ºC, respectively (15).…”

Section: Enzyme Characterizationmentioning

confidence: 92%

“…In this way, the results indicated that both glucoamylase and α-glucosidase may be secreted into the cultivation medium by A. flavus. The presence of both enzymes has been reported in culture media of A. awamori, A. niger and A. oryzae (18,19,20) and it was determined that the α-glucosidase from these fungi hydrolyses not only maltose and malto-oligosaccharides, but also hydrolyses soluble starch very slowly, while glucoamylase is a starch-hydrolase capable of also degrading starch (6).…”

Section: Effect Of Carbon Source Media Initial Ph and Temperature Ofmentioning

confidence: 99%

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Production of thermostable glucoamylase by newly isolated Aspergillus flavus A 1.1 and Thermomyces lanuginosus A 13.37

Gomes¹,

Souza²,

Grandi³

et al. 2005

Braz. J. Microbiol.

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Thirteen thermophilic fungal strains were isolated from agricultural soil, tubers and compost samples in tropical Brazil. Two strains were selected based on of their ability to produce considerable glucoamylase activity while growing in liquid medium at 45ºC with starch as the only carbon source. They were identified as Aspergillus flavus A1.1 and Thermomyces lanuginosus A 13.37 Tsiklinsky. The experiment to evaluate the effect of carbon source, temperature and initial pH of the medium on enzyme production was developed in a full factorial design (2x2x3). Enzyme productivity was influenced by the type of starch used as carbon source. Cassava starch showed to be a better substrate than corn starch for glucoamylase production by A. flavus but for T. lanuginosus the difference was not significant. Enzyme activities were determined using as substrates 0.3% soluble starch, 0.3% maltose or 0.3% of starch plus 0.1% maltose. The enzymes from A. flavus A1.1 hydrolyzed soluble starch preferentially but also exhibited a significant maltase activity. Moreover higher quantities of glucose were released when the substrate used was a mixture of starch and maltose, suggesting that this fungus produced two types of enzyme. In the case T. lanuginosus A 13.37, the substrate specificity test indicated that the enzyme released also hydrolyzed starch more efficiently than maltose, but there was no increase in the liberation of glucose when a mixture of starch and maltose was used as substrate, suggesting that only one type of enzyme was secreted. Glucoamylases produced from A. flavus A1.1 and T. lanuginous A.13-37 have high optimum temperature (65ºC and 70ºC) and good thermostability in the absence of substrate (maintaining 50% of activity for 5 and 8 hours, respectively, at 60ºC) and are stable over in a wide pH range. These new strains offer an attractive alternative source of enzymes for industrial starch processing.

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Section: Enzyme Characterizationmentioning

confidence: 92%

Section: Effect Of Carbon Source Media Initial Ph and Temperature Ofmentioning

confidence: 99%

Production of thermostable glucoamylase by newly isolated Aspergillus flavus A 1.1 and Thermomyces lanuginosus A 13.37

Gomes¹,

Souza²,

Grandi³

et al. 2005

Braz. J. Microbiol.

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“…However with further increase in the gene copy numbers, the glucoamylase yield decreased gradually and recombinant strains became genetically unstable. The fermentation of the recombinant strain A. niger B1 bearing 20 copies of the glucoamylase gene was performed to obtain a maximal glucoamylase production of 1510 mg/(g•h) at a maximal growth rate [19]. The multi-copy glucoamylase gene from bacterium was integrated into the chromosome of strains A. awamori and A. niger [20] glucoamylase activities of recombinant strains in the liquid fermentation were 2-fold higher compared to the original strain, and they were improved by 85% in the solid-state fermentation.…”

Section: Use Of the Strong Promoter To Improve The Production Of Indumentioning

confidence: 99%

Advanced Strategies for Improving the Production of Industrial Enzymes in Heterologous Host Systems

Chen¹

2013

Enz Eng

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Industrial enzymes, such as glucoamylase and amylase etc., are important biocatalysts which are widely used in many fields. In this paper, advanced strategies for improving the production of industrial enzymes in heterologous host systems were reviewed from the following aspects: the introduction of the strong promoter, the increase in the copy number of genes, the alternative to the signal peptide and the use of preferred codons.

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“…DNA fragments were separated by gel electrophoresis and Southern analysis was carried out as described by Swift et al [11]. Membranes were probed with digoxigenin (DIG) labelled niaD or glaA genes following the Boehringer Mannheim DIG chemiluminescent protocol with high stringency washes.…”

Section: Southern Analysismentioning

confidence: 99%

“…DNA was extracted from fungal mycelium according to the method of Swift et al [11] and was digested with XbaI at 37³C. DNA fragments were separated by gel electrophoresis and Southern analysis was carried out as described by Swift et al [11].…”

Section: Southern Analysismentioning

confidence: 99%

Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum

Gordon

2001

FEMS Microbiology Letters

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Fusarium venenatum JeRS 325, a strain which produces recombinant glucoamylase under control of a growth rate independent promoter was transformed with a plasmid carrying the Aspergillus niger glucoamylase gene under control of its own growth rate correlated promoter. Some disruption of the original recombinant genes occurred and at pH 5.8 the double transformant did not produce as much glucoamylase as JeRS 325 in batch culture. However, the double transformant still produced as much glucoamylase as JeRS 325 in fed-batch cultures, illustrating the potential for the combined use of growth rate independent and dependent promoters to improve production of recombinant proteins in fed-batch culture systems. ß

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Recombinant Glucoamylase Production byAspergillus nigerB1 in Chemostat and pH Auxostat Cultures

Cited by 39 publications

References 35 publications

Production of thermostable glucoamylase by newly isolated Aspergillus flavus A 1.1 and Thermomyces lanuginosus A 13.37

Production of thermostable glucoamylase by newly isolated Aspergillus flavus A 1.1 and Thermomyces lanuginosus A 13.37

Advanced Strategies for Improving the Production of Industrial Enzymes in Heterologous Host Systems

Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum

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