Isolation, partial purification, and some properties of protease I from a thermophilic mold Thermoascus aurantiacus var. levisporus

Marcy, R; Engelhardt, T. C.; Upadhyay, J.

doi:10.1007/bf00436630

Cited by 8 publications

(4 citation statements)

References 32 publications

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“…Similar results were reported for proteases from Thermoascus aurantiacus var. levisporus (55°C) (Marcy et al, 1984). Proteases from thermophilic Scytalidium (Hasbay and Ögel, 2002) and thermotolerant Aspergillus fumigatus (Santos et al, 1996) showed optimal activities at 45°C.…”

Section: Temperature (°C)mentioning

confidence: 98%

Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.

et al. 2010

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Thermophilic fungi produce thermostable enzymes which have a number of applications, mainly in biotechnological processes. In this work, we describe the characterization of a protease produced in solidstate (SSF) and submerged (SmF) fermentations by a newly isolated thermophilic fungus identified as a putative new species in the genus Myceliophthora. Enzyme-production rate was evaluated for both fermentation processes, and in SSF, using a medium composed of a mixture of wheat bran and casein, the proteolytic output was 4.5-fold larger than that obtained in SmF. Additionally, the peak of proteolytic activity was obtained after 3 days for SSF whereas for SmF it was after 4 days. The crude enzyme obtained by both SSF and SmF displayed similar optimum temperature at 50 degrees C, but the optimum pH shifted from 7 (SmF) to 9(SSF). The alkaline protease produced through solid-state fermentation (SSF), was immobilized on beads of calcium alginate, allowing comparative analyses of free and immobilized proteases to be carried out. It was observed that both optimum temperature and thermal stability of the immobilized enzyme were higher than for the free enzyme. Moreover, the immobilized enzyme showed considerable stability for up to 7 reuses.

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Section: Temperature (°C)mentioning

confidence: 98%

Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.

et al. 2010

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“…Protease activity was determined using a modified ANSON method [8]. The reaction mixture contained 1 ml of the enzyme solution and 5 ml of 0.6y0 HAMMARSTEN casein in 0.1 M phosphate buffer (pH 7.2).…”

Section: Enzyme Assaymentioning

confidence: 99%

The activities of partially purified acid proteases of thermotolerant Aspergillus species from post harvest oil palm kernels

Ogundero

1989

Nahrung

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The production and activities of extracellular acid proteases of Aspergiliusjmigutus Fres. and Aspergillus niduluns (Eidum) Win1 were studied. Both species grew readily on the palm kernel oil-peptone medium resulting in peak protease production and biomass accumulation occurring within the incubation period of 10 dys. Partial purification of the crude protease from the culture filtrate of A . fwnigutus on DEAE-cellulose and on Sephadex G-200 gave a single active protease peak being eluted with thF protein front ?t A,,,.A 47-fold purification was achieved with a recovery value of 2.1 %. The specific activity (22.4 U/mg protein) of A . fGmigatus protease was much higher than that of A . niduiuns protease (11.4 U/mg protein). Also, A . fumigatus protease was most active at 40 "C and pH 5.8 on casein and on gelatin. A . niduluns protease acted best at 45 "C and pH 5.4 on similar substrate. The proteases from both fungi showed no exoprotease activity when used to hydrolyze leucine amide, hippuryl phenylalanine and hippuryl arginine.

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“…Total protease activity was determined using the modified ANSON method [9]. The reaction mixture contained 1 ml of enzyme solution and 5 ml of 0.6",, HAMMARSTEN casein in 0.1 M phosphate buffer (pH 5.4).…”

Section: Growth and Crude Enzyme Productionmentioning

confidence: 99%

Proteolysis by toxigenic Aspergillus nidulans from Nigerian palm produce

1987

Nahrung

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The submerged cultures of Aspergillus nidulans had optimal growth and protease production at 37 degrees C and within 6 days of incubation. A rapid drop in pH of the growth medium from 6.9 to 4.8 and a subsequent gradual rise was recorded with the period of incubation. The acid-protease produced was purified by a combination of ethanolic precipitation, ultrafiltration and fractionation on DEAE-cellulose and Sephadex G-200. A single peak showing protease activity was subsequently obtained with a 16-fold increase in specific activity and a recovery value of 36%. The purified enzyme had optimal activity on casein and gelatin at pH 5.4 and a temperature of 40 degrees C.

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Isolation, partial purification, and some properties of protease I from a thermophilic mold Thermoascus aurantiacus var. levisporus

Cited by 8 publications

References 32 publications

Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.

Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.

The activities of partially purified acid proteases of thermotolerant Aspergillus species from post harvest oil palm kernels

Proteolysis by toxigenic Aspergillus nidulans from Nigerian palm produce

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