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Cited by 35Enzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationAdvanced Scientific Research Methods

Purification, structural characterization, and technological properties of an aspartyl proteinase from submerged cultures of Mucor mucedo DSM 809

Yegin, Sirma, Goksungur, Yekta, Fernandez-Lahore, Marcelo·2012·Food Chemistry
DOI 10.1016/j.foodchem.2012.01.075
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Abstract

An extracellular aspartyl proteinase from Mucor mucedo DSM 809 submerged cultures was purified by a two-steps chromatographic procedure. The enzyme had a molecular weight (MW) of 32.7kDa, and an isoelectric point (pI) value of 4.29; no evidence of N-linked glycosylation was found. As judged by mass spectrometry, the primary structure of the M. mucedo enzyme presented homology with Rhizopus spp. proteinases. The secondary structure showed 4% α-helix, 48% β-sheet and 48% random coil structure in 20mM phosphate buffer (pH 5.8), as evidenced by circular dichroism spectroscopy. When acting on milk to provoke curd formation, the proteinase showed maximum potency at pH 5.0 and at 40°C. The enzyme was heat-sensitive and became completely inactivated after incubation at 55°C for 10min. These results indicate that the milk-clotting enzyme from M. mucedo can be considered as a potential substitute for bovine chymosin in cheese manufacturing.

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Crossref · 10.1016/j.foodchem.2012.01.075

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  • Most studies have used liquid-state fermentation, regardless of the group of microorganisms.

    “Most studies have used LSF, regardless of the group of microorganisms (Shieh et al., 2009;Yegin et al., 2012;Acha et al., 2014;Sun et al., 2014;Ayana et al., 2015;Morillo et al., 2015;Guleria et al., 2016;Hang et al., 2016;Kumari Narwal et al., 2016;Lemes et al., 2016;Meng et al., 2018;Li et al., 2019;Putranto et al., 2019;Zhao et al., 2019;Zhang et al., 2019Zhang et al., , 2021Zhang et al., , 202”

    From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Yegin et al., 2012

  • Changing the temperature to 45°C caused instability in the Mucor mucedo enzyme, and the enzyme became completely inactive after reaching 50°C, suggesting a high sensitivity to heat.

    “Changing the temperature to 45°C caused instability in the enzyme, and the enzyme became completely inactive after reaching 50°C, suggesting a high sensitivity to heat.”

    From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Yegin et al., 2012

  • At 25°C, only 40% of the relative activity of the enzyme produced by Mucor mucedo was recorded.

    “At 25°C, only 40% of the relative activity of the enzyme produced by this mold was recorded.”

    From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Yegin et al., 2012

  • Even minimal activity of conventional rennet stored in curd can lead to extensive proteolysis, resulting in taste and odor defects, especially in the production of soft and semi-hard cheese types.

    “Even minimal activity of conventional rennet stored in curd can lead to extensive proteolysis, resulting in taste and odor defects, especially in the production of soft and semi-hard cheese types (Yegin et al., 2012).”

    From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Yegin et al., 2012

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Authors
Yegin, S., Goksungur, Y., & Fernandez-Lahore, M.
Venue
Food Chemistry
Publisher
Elsevier BV
Published
2012-08
Volume
133
Issue
4
Pages
1312-1319
ISSN
0308-8146 (ISSN-L)
DOI
10.1016/j.foodchem.2012.01.075
OpenAlex
W1970498581
Cited by
35
References
30
Citations by year
2026: 1 · 2025: 3 · 2023: 3 · 2021: 6 · 2020: 3 · 2019: 5 · 2018: 1 · 2017: 3 · 2016: 3 · 2015: 1 · 2014: 3 · 2013: 2 · 2012: 1
FWCI
1.99
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
Food Chemistry (publishedVersion)
Funders
Bundesministerium für Bildung und Forschung
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 › Agricultural and Biological Sciences › Food Science › Advanced Scientific Research Methods
Keywords
aspartic protease, Mucor mucedo, extracellular enzymes, enzyme purification, protein secondary structure, milk coagulation, cheese production, heat sensitivity, submerged culture

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