A novel serine protease with caspase- and legumain-like activities from edible basidiomycete Flammulina velutipes

Iketani, Aya; Nakamura, Mayumi; Suzuki, Yuya; Awai, Kazuo; Shioi, Yuzo

doi:10.1016/j.funbio.2013.01.005

Cited by 7 publications

(6 citation statements)

References 38 publications

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“…Interestingly, Pfam database includes more than 600 fungal S41 representatives, whereas MEROPS only 4 from 3 taxa: Cladophialophora immunda , Cordyceps bassiana and Sebacina vermifera . A recent article by Iketani and colleagues sheds some light on probable caspase-like function of S41 members based on the Agaricomycotina-conserved protein from Flammulina velutipes 32 .…”

Section: Resultsmentioning

confidence: 99%

Fungal lifestyle reflected in serine protease repertoire

Muszewska

Stepniewska-Dziubinska

Steczkiewicz

et al. 2017

Sci Rep

114

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Fungi are able to switch between different lifestyles in order to adapt to environmental changes. Their ecological strategy is connected to their secretome as fungi obtain nutrients by secreting hydrolytic enzymes to their surrounding and acquiring the digested molecules. We focus on fungal serine proteases (SPs), the phylogenetic distribution of which is barely described so far. In order to collect a complete set of fungal proteases, we searched over 600 fungal proteomes. Obtained results suggest that serine proteases are more ubiquitous than expected. From 54 SP families described in MEROPS Peptidase Database, 21 are present in fungi. Interestingly, 14 of them are also present in Metazoa and Viridiplantae – this suggests that, except one (S64), all fungal SP families evolved before plants and fungi diverged. Most representatives of sequenced eukaryotic lineages encode a set of 13–16 SP families. The number of SPs from each family varies among the analysed taxa. The most abundant are S8 proteases. In order to verify hypotheses linking lifestyle and expansions of particular SP, we performed statistical analyses and revealed previously undescribed associations. Here, we present a comprehensive evolutionary history of fungal SP families in the context of fungal ecology and fungal tree of life.

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Section: Resultsmentioning

confidence: 99%

Fungal lifestyle reflected in serine protease repertoire

Muszewska

Stepniewska-Dziubinska

Steczkiewicz

et al. 2017

Sci Rep

114

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“…The supernatant of F. velutipes contained numerous gelatin-cleaving peptidases that were not purified yet, 17 a glutaminase (85 kDa with 13 kDa subunits indicating a hexameric protein) 23 and a serine protease (34.5 kDa) with caspase-and legumain-like activities. 24 Flavourzyme is a commercial enzyme preparation of A. oryzae with endo-and exopeptidolytic activity. So far, the sequence analysis of peptidases of A. oryzae demonstrated about 18 peptidases, while the genome of A. oryzae was supposed to code for 134 putative peptidases.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The supernatant of F. velutipes contained numerous gelatin-cleaving peptidases that were not purified yet, a glutaminase (85 kDa with 13 kDa subunits indicating a hexameric protein) and a serine protease (34.5 kDa) with caspase- and legumain-like activities . Flavourzyme is a commercial enzyme preparation of A.…”

Section: Resultsmentioning

confidence: 99%

Factors Limiting the Enzymatic Hydrolysis of Wheat Gluten

Giesler

Linke

Berger

2014

J. Agric. Food Chem.

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The enzymatic hydrolysis of wheat gluten for the production of seasonings using mixtures of endo- and exopeptidases results in yields typically below 40%. Possible limiting parameters, such as an increasing product inhibition, autopeptidolysis of the enzymes, and lack of cleavage sites, were studied using novel peptidases from Flammulina velutipes or the commercial Flavourzyme preparation. Seven intermittent electrodialysis steps (10 g/L gluten and 10 kaU/mL) for the in situ removal of amino acids minimized the product inhibition. During 16 h, hydrolysis progressed nearly linearly. Compared to the batch control, a 3-fold yield of amino acids released was obtained indicating that an integrated product removal alleviates the problem of product inhibition. Autopeptidolysis, as shown using sodium dodecyl sulfate polyacrylamide gel electrophoresis and enzyme activity assays, was suppressed with increasing concentrations of competing gluten substrate. Peptidases of F. velutipes showed product inhibition only, whereas a combined effect of product inhibition and lack of cleavage sites was observed for Flavourzyme.

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“…The S41 peptidase could be involved in the formation of arginyl-peptides. To our knowledge, only one other fungal S41 peptidase has been described in the literature . S53 tripeptidyl-peptidases release tripeptides and are involved in the formation of small peptides .…”

Section: Resultsmentioning

confidence: 99%

“…To our knowledge, only one other fungal S41 peptidase has been described in the literature. 42 S53 tripeptidyl-peptidases release tripeptides and are involved in the formation of small peptides. 40 To our knowledge, a few of these peptidases were found in fungi, such as Rhizopus 43 and Aspergillus, 44 but not in basidiomycetes.…”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 99%

Salt Taste Enhancing l-Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota

Harth

Krah

Linke

et al. 2016

J. Agric. Food Chem.

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Some l-arginyl dipeptides were recently identified as salt taste enhancers, thus opening the possibility to reduce dietary sodium uptake without compromising palatability. A screening of 15 basidiomycete fungi resulted in the identification of 5 species secreting a high peptidolytic activity (>3 kAU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that l-arginyl dipeptides were liberated when casein or lysozyme served as substrate. Much higher yields of dipeptides (42-75 μmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest l-arginyl dipeptide yields and a significant salt taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and nonspecific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.

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A novel serine protease with caspase- and legumain-like activities from edible basidiomycete Flammulina velutipes

Cited by 7 publications

References 38 publications

Fungal lifestyle reflected in serine protease repertoire

Fungal lifestyle reflected in serine protease repertoire

Factors Limiting the Enzymatic Hydrolysis of Wheat Gluten

Salt Taste Enhancing l-Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota

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