ArticleJournal of industrial microbiology & biotechnology2016
Evaluation of the catalytic specificity, biochemical properties, and milk clotting abilities of an aspartic peptidase from Rhizomucor miehei.
Article in Journal of industrial microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 36 citations in OpenAlex.
- Unveiling the psychrozyme potential of micro-fungi inhabiting the high altitude passes of the trans-Himalayas.Biotechnology letters · 2025Article
- Characterization of a novel aspartic protease from Trichoderma asperellum for the preparation of duck blood peptides.Applied microbiology and biotechnology · 2024Article
- Fungal Proteases as Emerging Biocatalysts to Meet the Current Challenges and Recent Developments in Biomedical Therapies: An Updated Review.Journal of fungi (Basel, Switzerland) · 2022Review
- Characterization of a Novel Aspartic Protease fromFoods (Basel, Switzerland) · 2021Article
- Microbial proteases: ubiquitous enzymes with innumerable uses.3 Biotech · 2021Review
- Proteolytic analysis of Trichoderma reesei in celluase-inducing condition reveals a role for trichodermapepsin (TrAsP) in cellulase production.Journal of industrial microbiology & biotechnology · 2019Article
- Genome mining for peptidases in heat-tolerant and mesophilic fungi and putative adaptations for thermostability.BMC genomics · 2018Article
- Specificity of peptidases secreted by filamentous fungi.Bioengineered · 2018Review
- Enzymatic Synthesis of Protein Hydrolysates From Animal Proteins: Exploring Microbial Peptidases.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we detail the specificity of an aspartic peptidase from Rhizomucor miehei and evaluate the effects of this peptidase on clotting milk using the peptide sequence of k-casein (Abz-LSFMAIQ-EDDnp) and milk powder. Molecular mass of the peptidase was estimated at 37 kDa, and optimum activity was achieved at pH 5.5 and 55 °C. The peptidase was stable at pH values ranging from 3 to 5 and temperatures of up 45 °C for 60 min. Dramatic reductions in proteolytic activity were observed with exposure to sodium dodecyl sulfate, and aluminum and copper (II) chloride. Peptidase was inhibited by pepstatin A, and mass spectrometry analysis identified four peptide fragments (TWSISYGDGSSASGILAK, ASNGGGGEYIFGGYDSTK, GSLTTVPIDNSR, and GWWGITVDRA), similar to rhizopuspepsin. The analysis of catalytic specificity showed that the coagulant activity of the peptidase was higher than the proteolytic activity and that there was a preference for aromatic, basic, and nonpolar amino acids, particularly methionine, with specific cleavage of the peptide bond between phenylalanine and methionine. Thus, this peptidase may function as an important alternative enzyme in milk clotting during the preparation of cheese.
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