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. and Vrasanska, M. (1998): Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882. Carbohydr. Res. 306 , 445-455. Biochemical and catalytic properties

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Rezessy-Szabó, J. M., Nguyen, D. Q. & Hoschke, Á. (2000): Formation of α-galactosidase enzyme by Thermomyces lanuginosus. Fourteenth Forum for Applied Biotechnology. 27-28 September 2000. Gent, Belgium Proceedings part I, pp. 319

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Purkarthofer, H. and Steiner, W. 1995: Induction of endo-beta-xylanase in the fungus Thermomyces lanuginosuspp. Enzyme Microb. Technol. 17 , 114-118. Induction of endo-beta-xylanase in the fungus Thermomyces lanuginosus

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References Alam , M. , Gomes , I. , Mohuiddin , G. and Hoq , M. M. ( 1994 ): Production and characterization of thermostable xylanase by Thermomyces lanuginosus

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Arnesen, S., Eriksen, S. H., Olsen, J., Jensen, B. (2002) De novo synthesis is involved in production of extracellular α-amylase activity from Thermomyces lanuginosus in stationary phase. Mycol. Res. 106 , 345

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). Thermomyces lanuginosus was first isolated from soil and involved in compost degradation until its first isolation as plant endophyte ( Novas & Carmarán, 2008 ). The plants under extreme temperatures exhibit various symptoms like chlorosis and necrosis

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Ten different strains of Thermomyces lanuginosus , isolated from composting soils were found to produce phytase when grown on PSM medium. The wild type strain CM was found to produce maximum amount of phytase (4.33 units/g DW substrate). Culturing T. lanuginosus strain CM on medium containing wheat bran and optimizing other culture conditions (carbon source, media type, nitrogen source, level of nitrogen, temperature, pH, inoculum age, inoculum level and moisture), increased the phytase yield to 13.26 units/g substrate. This culture was further subjected to UV mutagenesis for developing phytase hyperproducing mutants. The mutant (TL-7) showed 2.29-fold increase in phytase activity as compared to the parental strain. Employing Box-Behnken factor factorial design of response surface methodology resulted in optimized phytase production (32.19 units/g of substrate) by mutant TL-7. A simple two-step purification (40.75-folds) of phytase from mutant TL-7 was achieved by anion exchange and gel filtration chromatography. The purified phytase (∼54 kDa) was characterized to be optimally active at pH 5.0 and temperature 70 °C, though the enzyme showed ∼70% activity over a wide pH and temperature range (2.0–10.0 and 30–90 °C, respectively). The phytase showed broad substrate specificity with activity against sodium phytate, ADP and riboflavin phosphate. The phytase from T. lanuginosus was thermoacidstable as it showed up to 70% residual activity after exposure to 70 °C at pH 3.0 for 120 min. The enzyme showed K m 4.55 μM and V max 0.833 μM/min/mg against sodium phytate as substrate.

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Agrokémia és Talajtan
Authors: Mária Óbert, Antalné Csepregi, Katalin Posta, Erika Tóth Király and László Hornok

Szennyvíziszapból és lignocellulóz-tartalmú növényi hulladékból álló, termofil fázisban lévő komposzthalmokból 21 gombát izoláltunk. A morfológiai és molekuláris módszerekkel azonosított gombák tíz fajba tartoztak, hat termofil fajba ( Aspergillus fumigatus, Aspergillus versicolor, Rhizomucor pusillus, Thermoascus aurantiacus, Talaromyces thermophilus, Thermomyces lanuginosus ) és négy mezofilbe ( Aspergillus oryzae, Aspergillus terreus, Neosartorya fischerii és Trichoderma hamatum ). A két leggyakoribb faj a T. lanuginosus és a T. thermophilus volt, az előbbit nyolc, az ut_

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Thermomyces lanuginosus . Biochim. Biophys. Acta 1524 , 27–37. Biely P. Purification and characterization of α-galactosidase from a thermophilic fungus Thermomyces lanuginosus

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from the culture filtrate of Thermomyces lanuginosus ATCC 46882. Carbohydr. Res. 306 , 445–455. Bhat M. K. Biochemical and catalytic properties of an endoxylanase purified from the

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