Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626

Nguyen, Quang D.; Rezessy‐Szabó, Judit M.; Claeyssens, Marc; Stals, Ingeborg; Hoschke, Ágoston

doi:10.1016/s0141-0229(02)00128-x

Cited by 143 publications

(69 citation statements)

References 14 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: 85%

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: 85%

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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show abstract

“…Um fato interessante, é que, mesmo entre os mesófilos, que crescem entre 28 e 32 °C, é possível encontrar enzimas que atuam em temperaturas até 30 °C acima da temperatura máxima de crescimento do organismo produtor, como a glucoamilase de Neosartorya fischeri, que atua a 60 °C 91 . A α-amilase produzida pela linhagem Thermomyces lanuginosus ATCC 34626 apresentou meia vida a 60 °C por 1 dia 108 . Observa-se que não existe diferença muito pronunciada entre as termoestabilidades e as temperaturas de atividade ótima das amilases produzidas por fungos termófilos e alguns mesófilos.…”

Section: Amilases Termoestáveisunclassified

Enzimas termoestáveis: fontes, produção e aplicação industrial

et al. 2007

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“…A variety of downstream processing techniques such ion exchange chromatography, hydrophobic interaction chromatography, and gel filtration chromatography have been exploited for the purification of glucoamylase [1,[7][8][9][10][11]. But the flipside of these procedures is that they are expensive, time consuming, and are often multistep low-yield protocols, not suitable for large scale production.…”

Section: Introductionmentioning

confidence: 99%

Partitioning of thermostable glucoamylase in polyethyleneglycol/salt aqueous two-phase system

Vinayagam

Murty

2015

Bioresour. Bioprocess.

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Background: A major challenge in downstream processing is the separation and purification of a target biomolecule from the fermentation broth which is a cocktail of various biomolecules as impurities. Aqueous two phase system (ATPS) can address this issue to a great extent so that the separation and partial purification of a target biomolecule can be integrated into a single step. In the food industry, starch production is carried out using thermostable glucoamylase. Humicola grisea serves as an attractive source for extracellular production of glucoamylase. Results: In the present investigation, the possibility of using polyethylene glycol (PEG)/salt-based ATPS for the partitioning of glucoamylase from H. grisea was investigated for the first time. Experiments were conducted based on one variable at a time approach in which independent parameters like PEG molecular weight, type of phase-forming salt, tie line length, phase volume ratio, and neutral salt concentration were optimized. It has been found that the PEG 4000/potassium phosphate system was suitable for the extraction of glucoamylase from the fermentation broth. From the results, it was observed that, at a phase composition of 22 % w/w PEG 4000 and 12 % w/w phosphate in the presence of 2 % w/w NaCl and at pH 8, glucoamylase was partitioned into the salt-rich phase with a maximum yield of 85.81 %.

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Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626

Cited by 143 publications

References 14 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

Enzimas termoestáveis: fontes, produção e aplicação industrial

Partitioning of thermostable glucoamylase in polyethyleneglycol/salt aqueous two-phase system

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