Production of thermostable β-mannosidase by a strain of Thermoascus aurantiacus: Isolation, partial purification and characterization of the enzyme

Microbial Mannanases: Properties and Applications

“…1998 ;Perret et al 2004 ). Gomes et al ( 2007 ) achieved the highest β-mannanase and β-mannosidase activity by the thermophilic fungus ( Thermoascus aurantiacus ) with soya meal as nitrogen source, supplemented with LBG as carbon source. Recently, Mohamad et al .…”

“…Mannanase production by microorganisms is infl uenced by the media composition, mostly carbon and nitrogen (Kataoka and Tokiwa 1998 ;Dhawan and Kaur 2007 ). Groβwindhager et al ( 1999 ) used glucose and cellulose for S. rolfsii , while Ademark et al ( 1998 ) and Gomes et al ( 2007 ) used locust bean gum (LBG) for A. niger and a thermophilic fungus, Thermoascus aurantiacus . Ferreira and Filho ( 2004 ) have used wheat bran as the carbon source for the production of β-mannanase from mesophilic fungus Trichoderma harzianum strain T4.…”

Predominant allylic hydroxylation at carbons 6 and 7 of 4 and 5-ene functionalized steroids by the thermophilic fungus Rhizomucor tauricus IMI23312

“…progesterone (1), androst-4-en-3,17-dione (2) and pregnenolone (13) Following 6 h incubation of progesterone (1) the 1 H NMR spectrum of the extract contained a resonance signal at 4.36 ppm (t) consistent with 6␣-H following hydroxylation at C-6␤. The 11␤-H resonance signal at 4.56 ppm (td) was present at 24 h. Methyl signals in the same spectrum at 0.73 ppm (18-H) and 1.79 ppm (19-H) were consistent with the isolated dihydroxylation product 5.…”

“…proteases, lipases, amylases, cellulases, xylanases) and cell associated enzymes (e.g. trehalase, invertase, ␤-glycosidase) [1][2][3]. The majority of these enzymes have high temperature stability and tolerance to a wide range of pH [1].…”

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

“…39,40) Similarly, the K mapp value (0.48 mM) of -D-mannosidase for p-nitrophenyl--D-mannoside is comparable to those reported (from 0.18 to 3.1 mM) for the same enzyme from other fungi, including T. reesei 42) and Thermoascus aurantiacus. 43) In the case of the endo-1,4--D-mannanase, kinetic comparisons are difficult, since the polymeric chains of galactomannans vary in respect of the length and degree of substitution, depending on their source. Nevertheless, the K mapp value (0.49 mg/ml) of endo-1,4--D-mannanase for guar galactomannan was lower than those reported for T. reesei (1.5 mg/ml) 44) and Trichoderma harzianum (1.3 mg/ml) 45) for locust bean gum mannan and guar galactomannan, respectively; however, close K mapp values (0.23 to 0.55 mg/ml) have been reported for bacterial endo-1,4--D-mannanases from Caldocellum saccharolyticum 46) and Thermotoga neapolitana, 47) using azocarob galactomannan and locust bean gum as substrates.…”