Aspartic proteinase from Penicillium camemberti: Purification, properties, and substrate specificity

Chrzanowska, Józefa; Kolaczkowska, M.; Dryjanski, Marek; Stachowiak, Damian; Polanowski, Antoni

doi:10.1016/0141-0229(94)00129-f

Cited by 24 publications

(17 citation statements)

References 24 publications

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“…In the temperature range of 45-55°C was observed activity levels higher than 50%, while out of this interval a rapid decrease was verified. An optimum temperature of 50°C was also reported for other aspartyl proteases, such as from Neosartorya fischeri (Wu and Hang 1998), Penicillium camemberti (Chrzanowska et al 1995), Mucor rouxii (Diaz and Ruiz Herrera 1987) and Hebeloma crustuliniforme (Zhu et al 1990). Nevertheless, the acid protease of Aspergillus oryzae showed optimum temperature at 55°C (Vishwanatha et al 2009).…”

Section: Effect Of Ph and Temperature On The Activity And Ph Stabilitymentioning

confidence: 85%

“…This optimum pH is similar to those reported to aspartic protease from Rhizophus oryzae (Kumar et al 2005) and Synergistes sp (Kumar et al 2008), but higher than the pH range (3.0-4.0) observed to acid protease from Aspergillus oryzae (Vishwanatha et al 2009). According to Chrzanowska et al (1995) in general, filamentous fungal acid proteases present optimum pH between 2.0 and 4.0.…”

Section: Effect Of Ph and Temperature On The Activity And Ph Stabilitymentioning

confidence: 99%

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Purification and some properties of an extracellular acid protease from Aspergillus clavatus

Silva

Knob²,

Tremacoldi

et al. 2011

World J Microbiol Biotechnol

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Acid proteases represent an important group of enzymes, widely used in food, beverage and pharmaceutical industries. For most of these applications the enzymatic preparation must be at least partially purified and free of substances that could change the characteristics of the product or the process. Fungal proteases have replaced other sources because they are easily obtained mainly from Mucor, Rhizopus, Penicillium and Aspergillus species. A strain of Aspergillus clavatus was selected by producing high level of acid protease activity. An extracellular aspartatic protease from this strain was purified 37.2 times with 37% recovery using (NH 4 ) 2 SO 4 fractionation and ionexchange chromatography. The enzyme was found to be monomeric having a molecular mass of 30.4 kDa. The purified enzyme is an acid protease with optimum pH of 5.5 and temperature for optimum activity of 50°C. Its high pH stability was verified in the range of 3.5-6.5. The acid protease was strongly inhibited by Hg ?2 and partially inhibited by Cu ?2 , Zn ?2 and Mn ?2 . The enzyme was sensitive to denaturing agent SDS and activated by thiolcontaining reducing agent dithiotreitol (DTT). The protease activity was not influenced by iodoacetic acid, E-64 and PMSF, while it was lightly actived by EDTA and totally inhibited by pepstatin, with a K i of 7.8 lM, indicating that is an aspartic protease. A. clavatus acid protease presents interesting characteristics for biotechnological process, such as cheese and flavor manufacture and dietary supplements, in which activity and stability in acid pH are required.

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Section: Effect Of Ph and Temperature On The Activity And Ph Stabilitymentioning

confidence: 85%

Section: Effect Of Ph and Temperature On The Activity And Ph Stabilitymentioning

confidence: 99%

Purification and some properties of an extracellular acid protease from Aspergillus clavatus

Silva

Knob²,

Tremacoldi

et al. 2011

World J Microbiol Biotechnol

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“…Optimum pH values between 3.0 and 5.5 have been reported for other fungi proteases, such as the one of Penicillium camemberti (pH 3.5) [42] and Rhizopus oryzae (pH 5.5) [43]. The A. niger NRRL 1785 protease exhibited an optimum at pH 4.0 [44].…”

Section: Discussionmentioning

confidence: 99%

Optimization of Acid Protease Production byAspergillus nigerI1 on Shrimp Peptone Using Statistical Experimental Design

Siala

Frikha

Mhamdi

et al. 2012

The Scientific World Journal

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Medium composition and culture conditions for the acid protease production byAspergillus nigerI1 were optimized by response surface methodology (RSM). A significant influence of temperature, KH2PO4, and initial pH on the protease production was evaluated by Plackett-Burman design (PBD). These factors were further optimized using Box-Behnken design and RSM. Under the proposed optimized conditions, the experimental protease production (183.13 U mL−1) closely matched the yield predicted by the statistical model (172.57 U mL−1) withR2=0.914. Compared with the initial M1 medium on which protease production was 43.13 U mL−1, a successful and significant improvement by 4.25 folds was achieved in the optimized medium containing (g/L): hulled grain of wheat (HGW) 5.0; KH2PO41.0; NaCl 0.3; MgSO4(7H2O) 0.5; CaCl2(7H2O) 0.4; ZnSO40.1; Na2HPO41.6; shrimp peptone (SP) 1.0. The pH was adjusted at 5 and the temperature at30°C. More interestingly, the optimization was accomplished using two cheap and local fermentation substrates, HGW and SP, which may result in a significant reduction in the cost of medium constituents.

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“…2). Optimal pH values for acid proteinases from other fungi vary from 2·0 to 4·0 (Choi et al 1991 ;Nizharadze et al 1991 ;Chrzanowska et al 1995 ;Ikasari and Mitchell 1996). The for the optimum pH; for pH stability, the relative activity for the optimum temperature; for thermal stability, the relative Fig.…”

Section: Effect Of Phmentioning

confidence: 99%

Purification and characterization of acid proteinase from Neosartorya fischeri var. spinosa IBT 4872

Hang

1998

Lett Appl Microbiol

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N G. 1998. An acid proteinase from Neosartorya fischeri var. spinosa IBT 4872 was purified 38-fold with a yield of 11% by ultrafiltration, ammonium sulphate fractionation, Sephadex-G200 gel filtration, DEAE-Sephadex anion exchange chromatography, and hydroxyapatite chromatography. The enzyme was most active at pH 3·0 and 50°C and had a molecular weight of 45 kDa, as determined by SDS-PAGE. It was stable over a pH range of 3·0 to 6·0 and exhibited thermal stability up to 50°C. The Km value for haemoglobin was 0·44% (w/v). The activity was inhibited by pepstatin, suggesting that the enzyme is an aspartic proteinase.

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Aspartic proteinase from Penicillium camemberti: Purification, properties, and substrate specificity

Cited by 24 publications

References 24 publications

Purification and some properties of an extracellular acid protease from Aspergillus clavatus

Purification and some properties of an extracellular acid protease from Aspergillus clavatus

Optimization of Acid Protease Production byAspergillus nigerI1 on Shrimp Peptone Using Statistical Experimental Design

Purification and characterization of acid proteinase from Neosartorya fischeri var. spinosa IBT 4872

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