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

Wu, Lauren; Hang, Y. D.

doi:10.1046/j.1472-765x.1998.00398.x

Cited by 11 publications

(14 citation statements)

References 15 publications

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“…The enzyme was stable over a wide range of pH from 3.5 to 6.5, but lost all activity at pH 2.0. Similar results were observed to acid proteases from Aspergillus niger (Singh et al 1994), A. oryzae (Vishwanatha et al 2009), Neosartorya fischeri (Wu and Hang 1998) and Rhizopus oryzae (Kumar et al 2005). In general, fungal acid proteases are stable between pH 2.5 and 6.0 (Rao et al 1998).…”

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

confidence: 57%

“…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: 61%

“…However, acid proteases characterized as aspartic-type of higher than these range have been found in other species such as 47.6 kDa from Aspergillus oryze (Vishwanatha et al 2009), 45 kDa from Neosartorya fischeri var. spinosa (Wu and Hang 1998) and 60 kDa from Synergistes sp. (Kumar et al 2008).…”

Section: Resultsmentioning

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 Stabilitysupporting

confidence: 57%

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

confidence: 61%

See 1 more Smart Citation

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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“…The optimal temperatures of the N. fischeri var. spinosa IBT 4872 acid protease (Wu and Hang 1998), Halophilic halobacterium sp. proteases from salted seaweed (An et al.…”

Section: Resultsmentioning

confidence: 99%

“…1991), pH 6.0–9.0 of the B. subtilis CCKS‐111 protease from soy sauce (Choi and Kim 1997) and pH 3.0–7.0 of the N. fischeri var. spinosa IBT 4872 acid protease (Wu and Hang 1998).…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of Bacillus Subtilis Jm-3 Protease From Anchovy Sauce

Kim

2005

J Food Biochemistry

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Bacillus subtilis JM‐3 was isolated from anchovy sauce naturally fermented in an underground cellar at 15 ± 3C for 3 years. The activity of the B. subtilis protease was highest in the 40–60% ammonium sulfate fraction. The yield of the purified protease was 5.3%, and its purification ratio was 35.6 folds. The molecular weight of the B. subtilis protease was 17.1 kDa, and its Km and Vmaxvalues were 1.75 μg/mL and 318 μM 1/min, respectively. The optimal temperature for protease activity was 60C, but optimal stability temperature was 30C. The optimal pH for protease activity and stability was 5.5. Therefore, the B. subtilis JM‐3 protease was classified as an acid protease. The relative activities of the B. subtilis JM‐3 protease were 69, 21 and 1.3% at 10, 20 and 30% NaCl concentrations, respectively. The best substrate for the B. subtilis JM‐3 protease was benzyloxycarbonyl‐glycine‐p‐nitrophenyl ester followed by bovine serum albumin. p‐Toluene‐sulfonyl‐L‐lysine chloromethylketone was the strongest inhibitor followed by soybean trypsin inhibitor, but N‐ethylmaleimide did not inhibit this enzyme. The B. subtilis JM‐3 protease was therefore presumed to be a trypsin‐like serine protease.

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Purification and characterisation of an acid protease from theAspergillus hennebergiiHX08 and its potential in traditional fermentation

Huang

Wang

2017

J. Inst. Brew.

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A protease AP3 from Aspergillus hennebergii HX08 was purified by ammonium‐sulphate precipitation, followed by anion‐exchange chromatography and gel filtration. The molecular weight of acid protease AP3 was 33 kDa (SDS‐PAGE and MALDI‐TOF‐MS). The protease AP3 was identified as an acid protease with MALDI‐TOF/TOF tandem MS. Its optimal temperature and pH were 60°C and 4.0, respectively. Its Kmax and Vmax were 57.92 mg/mL and 32.57 U/mL, respectively. The enzyme was active over a broad pH and temperature range (pH 3.0–5.0 and 30–60°C), and exhibited high activity and stability in 2–12% (v/v) ethanol solvent. Subsequent studies suggest that the enzyme presents a relatively high substrate affinity to wheat protein (98% of total activity). Its application to solid‐state fermentation of wheat flour with Saccharomyces cerevisiae could increase the hydrolysis degree of wheat protein (28.26%) and amino acid nitrogen concentration of fermented grains (34.21%). Additionally, enhanced S. cerevisiae biomass (37.09%) and alcohol concentration (38.29%) were also observed during the process. Volatile compounds analysis of fermented grains by headspace solid‐phase micro‐extraction and GC‐MS revealed more flavour compounds. These results suggest its potential in food and alcohol industries. Copyright © 2017 The Institute of Brewing & Distilling

show abstract

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

Cited by 11 publications

References 15 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

Purification and Characterization of Bacillus Subtilis Jm-3 Protease From Anchovy Sauce

Purification and characterisation of an acid protease from theAspergillus hennebergiiHX08 and its potential in traditional fermentation

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