• Title/Summary/Keyword: Thermoascus aurantiacus

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Enzyme Production Related to Alcohol Metabolism from Thermophilic Fungus Thermoascus aurantiacus (호열성 사상균 Thermoascus aurantiacus의 알코올분해대사 관련 효소학적 특성)

  • Ko Hee-Sun;Kim Hyun-Soo
    • Microbiology and Biotechnology Letters
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    • v.34 no.3
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    • pp.216-220
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    • 2006
  • Thermophillic fungus Thermoascus aurantiacus showed excellent growth and produced high amount of alcohol oxidase and catalase in a pectin medium. Besides, the strain produced enzymes which related with pectin or alcohol decomposition. We detected extracellular pectin esterase (EC 3.1.1.11) activity and, both intracellular and extracellular pectinase (EC 4.2.2.10) activity, as pectinolytic enzymes produced by T. aurantiacus. The production of methanol decomposition enzymes, such as alcohol oxidase (AOD, EC 1.1.3.13), alcohol dehydrogenase (ADH, EC 1.1.1.1), formaldehyde dehydrogenase (FADH, EC 1.2.1.1) and formate dehydrogenase (FDH, EC 1.2.1.2) follows by pectin esterase reaction which is converted to methanol. We concluded that T. aurantiacus has pectinolytic and alcohol - oxidative enzymological mechanism which produced carbon dioxide as a final material, started from pectin.

A Specific Short Dextrin-Hydrolyzing Extracellular Glucosidase from the Thermophilic Fungus Themoascus aurantiacus 179-5

  • Carvalho Ana Flavia Azevedo;Goncalves Aline Zorzetto;Silva Roberto da;Gomes Eleni
    • Journal of Microbiology
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    • v.44 no.3
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    • pp.276-283
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    • 2006
  • The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (${\alpha}$-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II ${\alpha}$-glucosidase. The optimum temperature of the enzyme was $70^{\circ}C$. In addition, the enzyme was highly thermostable (100% stability for 10 h at $60^{\circ}C$ and a half-life of 15 min at $80^{\circ}C$), and stable within a wide pH range.

Isolation and Analysis of the Enzymatic Properties of Thermophilic Fungi from Compost

  • Lee, Hanbyul;Lee, Young Min;Jang, Yeongseon;Lee, Sangjoon;Lee, Hwanhwi;Ahn, Byoung Jun;Kim, Gyu-Hyeok;Kim, Jae-Jin
    • Mycobiology
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    • v.42 no.2
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    • pp.181-184
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    • 2014
  • To the best of our knowledge, this is the first report on thermophilic fungi isolated in Korea. Three species of thermophiles were isolated from compost and were identified as Myriococcum thermophilum, Thermoascus aurantiacus, and Thermomyces lanuginosus. They can grow at temperatures above $50^{\circ}C$ and produce high levels of cellulolytic and xylanolytic enzymes at high temperatures. Notably, the considerable thermostability of the endo-glucanase produced by T. aurantiacus has made the fungus an attractive source of industrial enzymes.