Cited by 87Enzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationProtein Hydrolysis and Bioactive Peptides

Partial characterization of protease from a thermophilic fungus, Thermoascus aurantiacus, and its hydrolytic activity on bovine casein

Merheb, Carolina W., Cabral, Hamilton, Gomes, Eleni, Da-Silva, Roberto·2007·Food Chemistry

Abstract

Proteases are one of the most important groups of industrial enzymes, with considerable application in the food industry. The aim of this work was to study a novel protease produced by the thermophilic fungus, Thermoascus aurantiacus, through solid-state fermentation (SSF). The enzyme acted optimally at pH 5.5 and 60 °C; it was stable up to 60 °C for 1 h and in the pH range 3.0-9.5. To elucidate the enzyme's proteolytic activity, its hydrolytic profile on bovine casein, an important protein in the food industry, was studied by enzymatic hydrolysis on skim milk, analyzed by gel electrophoresis (UREA-PAGE), which clearly showed that the protease does not have the same specificity as bovine chymosin.

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Crossref · 10.1016/j.foodchem.2006.11.010

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  • Most aspartyl proteases synthesized by fungi exhibit the highest activity under acidic conditions.

    “as most aspartyl proteases synthesized by fungi exhibit the highest activity under acidic conditions.”
  • A broader range of stability has been observed for proteases derived from Rhizopus oryzae (pH 4.0 to 9.0), Thermoascus aurantiacus (pH 3.0 to 6.0), and Piptoporus soloniensis (pH 3.0 to 9.0).

    “A broader range of stability has been observed for proteases derived from R. oryzae (pH 4.0 to 9.0; Kumar et al., 2005), Thermoascus aurantiacus (pH 3.0 to 6.0; Merheb et al., 2007), and Piptoporus soloniensis (pH 3.0 to 9.0; El-Baky et al., 2011).”

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Authors
Merheb, C. W., Cabral, H., Gomes, E., & Da-Silva, R.
Affiliations
Instituto de Biociências, Letras e Ciências Exatas, câmpus de São José do Rio Preto (BR)
Venue
Food Chemistry
Publisher
Elsevier BV
Published
2007-01
Volume
104
Issue
1
Pages
127-131
ISSN
0308-8146 (ISSN-L)
OpenAlex
W1996381338
Cited by
87
References
29
Citations by year
2025: 4 · 2024: 2 · 2023: 4 · 2022: 6 · 2021: 2 · 2019: 3 · 2018: 5 · 2017: 6 · 2016: 3 · 2015: 6 · 2014: 7 · 2013: 8 · 2012: 5
FWCI
1.65
Type
journal article
Language
en
Open access
closed
Locations
  • Food Chemistry (publishedVersion)
  • Acervo Digital da Universidade Estadual Paulista (Universidade Estadual Paulista) (submittedVersion)
  • UNESP Institutional Repository (São Paulo State University) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
Keywords
proteolytic enzymes, Thermoascus aurantiacus, thermophilic fungi, solid-state fermentation, enzyme characterization, thermal stability, pH stability, proteolytic specificity, skim milk, industrial enzymes

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