Production and Purification of Acid Protease from the Thermophilic Fungus, Penicillium duponti K1014

Hashimoto, Hikotaka; Kaneko, Yukio; Iwaasa, Takashi; Yokotsuka, Tamotsu

doi:10.1128/aem.25.4.584-588.1973

Cited by 16 publications

(3 citation statements)

References 7 publications

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“…Among the advantages of enzyme production by fungi, its low cost, high productivity, fast production, and ease with which the enzymes can be modified are most concerned. Several studies have recently been performed on the isolation of acid proteases from different fungi such as Aspergillus saitoi, Aspergillus oryzae, − Aspergillus niger, , Mucor pusillus, Rhizopus hangchow, Monascus pilosus, − and Penicillium duponti . However, many reported activity levels were still poor.…”

Section: Introductionmentioning

confidence: 99%

“…Several studies have recently been performed on the isolation of acid proteases from different fungi such as Aspergillus saitoi, 5 Aspergillus oryzae, 6−8 Aspergillus niger, 9,10 Mucor pusillus, 11 Rhizopus hangchow, 12 Monascus pilosus, 13−15 and Penicillium duponti. 16 However, many reported activity levels were still poor. Therefore, new species for the production of acid proteases are still being sought by several scientists.…”

Section: ■ Introductionmentioning

confidence: 99%

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Characterization of Acidic Protease from Aspergillus niger BCRC 32720

Yin

Hsu

Jiang

2013

J. Agric. Food Chem.

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An acid protease from the broth of a 24 h cultivated Aspergillus niger BCRC 32720 was purified to electrophoretical homogeneity by CM Sepharose FF and Sephacryl S-100 HR chromatographs. The specific activity, purification fold, and yield were 23.29 kU/mg, 2.5, and 24.2%, respectively. Molecular mass (M) and N-terminal amino acid sequence were 47.5 kDa and SKGSAVTT, whereas the pH and temperature optima were at 2.5 and 50 °C, respectively. It was stable at pH 2.0-4.0 or ≤40 °C and activated by Fe(2+) and cysteine, but partially inhibited by phenylmethanesulfonyl fluoride and tosyllysine chloromethyl ketone and highly inhibited by Ag(+), Sn(2+), Fe(3+), Sb(3+), and pepstatin A. It was considered to be an aspartic protease.

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Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Characterization of Acidic Protease from Aspergillus niger BCRC 32720

Yin

Hsu

Jiang

2013

J. Agric. Food Chem.

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“…Milk-clotting acid proteases from thermophilic species of Mucor, Mucor pusillus (1, 10) and Mucor miehei (16,17), have been purified and characterized. However, the properties of acid protease from other thermophilic fungi have not been described in detail; only a few reports (4,5) have been published at this time.…”

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confidence: 99%

Some Properties of Acid Protease from the Thermophilic Fungus, Penicillium duponti K1014

Hashimoto

Iwaasa

Yokotsuka

1973

Applied Microbiology

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A purified acid protease from a true thermophilic fungus, Penicillium duponti K1014, was most active at pH 2.5 for milk casein and at pH 3.0 for hemoglobin. The enzyme was stable at a pH range of 2.5 to 6.0 at 30 C for 20 h. The acid protease retained full activity after 1 h at 60 C at a pH range between 3.5 and 5.5. At the most stable pH of 4.5, more than 65% of its activity remained after heat treatment for 1 h at 70 C. These thermal properties show the enzyme as a thermophilic protein. The enzyme activity was strongly inhibited by sodium lauryl sulfate and oxidizing reagents such as potassium permanganate and N-bromosuccinimide. No inhibition was caused by chelating reagents, potato inhibitor, and those reagents which convert sulfhydryl groups to mercaptides. Reducing reagents showed an activating effect. The enzyme showed the trypsinogen-activating property at an acidic pH range; optimal trypsinogen activation was obtained at a pH of approximately 3.0. The isoelectric point of the enzyme was estimated to be pH 3.89 by disk electrofocusing. By using gel filtration, an approximate value of 41,000 was estimated for the molecular weight.

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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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Production and Purification of Acid Protease from the Thermophilic Fungus, Penicillium duponti K1014

Cited by 16 publications

References 7 publications

Characterization of Acidic Protease from Aspergillus niger BCRC 32720

Characterization of Acidic Protease from Aspergillus niger BCRC 32720

Some Properties of Acid Protease from the Thermophilic Fungus, Penicillium duponti K1014

Proteolysis by toxigenic Aspergillus nidulans from Nigerian palm produce

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