A prolyl endopeptidase from Flammulina velutipes for the possible degradation of celiac disease provoking toxic peptides in cereal proteins

Schulz, Kathrin; Giesler, Lucienne; Linke, Diana; Berger, Ralf G.

doi:10.1016/j.procbio.2018.07.019

Cited by 14 publications

(17 citation statements)

References 35 publications

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“…Protein bands were excised from SDS gels, dried, and tryptically hydrolysed. The resulting peptides were extracted and purified according to standard protocols and the amino acid sequence was analyzed with electrospray ionization-tandem mass spectrometry (ESI-MS/MS) using a maXis quadrupole time of flight (QTOF) mass spectrometer (Bruker, Bremen, Germany) as described previously [43,44]. The obtained partial sequences of PsaPOX and of the oxidase were used for a similarity search against public databases (NCBI BlastP).…”

Section: Peptide Mass Fingerprintingmentioning

confidence: 99%

A DyP-Type Peroxidase of Pleurotus sapidus with Alkene Cleaving Activity

2020

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Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete Pleurotus sapidus (PsaPOX) cleaved the aryl alkene trans-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn2+-oxidation site on its surface. The gene was expressed in Komagataella pfaffii GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H2O2 and 25 mM Mn2+. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn2+ to Mn3+. In addition, bleaching of β-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (E)-methyl isoeugenol, α-methylstyrene, and trans-anethole, which was increased almost twofold in the presence of Mn2+. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production.

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Section: Peptide Mass Fingerprintingmentioning

confidence: 99%

A DyP-Type Peroxidase of Pleurotus sapidus with Alkene Cleaving Activity

2020

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“…Experimental strategies include reducing the immune response by modifying gluten in the diet of susceptible patients (Merz et al 2016;Scherf et al 2018) and enzyme therapy that supplements gluten-degrading enzymes in the GIT. Both approaches use peptidases from various sources such as fungi, bacteria, and germinated cereal grains (Curiel et al 2014;Guandalini and Assiri 2014;Wolf et al 2015;Scherf et al 2018;Schulz et al 2018). Postproline cutting prolyl endopeptidases from Sphingomonas capsulata, Flavobacterium meningosepticum, Myxococcus xanthus, Aspergillus niger, Flammulina velutipes, and Chryseobacterium taeanense, among others, have been pursued as drug candidates for the enzymatic treatment of gluten to treat celiac disease (Shan et al 2004;Mitea et al 2008;Schulz et al 2018;Amador et al 2019).…”

Section: Introductionmentioning

confidence: 99%

“…Both approaches use peptidases from various sources such as fungi, bacteria, and germinated cereal grains (Curiel et al 2014;Guandalini and Assiri 2014;Wolf et al 2015;Scherf et al 2018;Schulz et al 2018). Postproline cutting prolyl endopeptidases from Sphingomonas capsulata, Flavobacterium meningosepticum, Myxococcus xanthus, Aspergillus niger, Flammulina velutipes, and Chryseobacterium taeanense, among others, have been pursued as drug candidates for the enzymatic treatment of gluten to treat celiac disease (Shan et al 2004;Mitea et al 2008;Schulz et al 2018;Amador et al 2019). Although many digestive enzyme supplements are ineffective in degrading immunogenic gluten epitopes, prolyl endopeptidase from Aspergillus niger is able to degrade toxic gluten epitopes (Janssen et al 2015).…”

Section: Introductionmentioning

confidence: 99%

Microbiome of root vegetables—a source of gluten-degrading bacteria

Kõiv

Adamberg

et al. 2020

Appl Microbiol Biotechnol

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Gluten is a cereal protein that is incompletely digested by human proteolytic enzymes that create immunogenic peptides that accumulate in the gastrointestinal tract (GIT). Although both environmental and human bacteria have been shown to expedite gluten hydrolysis, gluten intolerance is a growing concern. Here we hypothesize that together with food, we acquire environmental bacteria that could impact our GIT with gluten-degrading bacteria. Using in vitro gastrointestinal simulation conditions, we evaluated the capacity of endophytic bacteria that inhabit root vegetables, potato (Solanum tuberosum), carrot (Daucus sativus), beet (Beta vulgaris), and topinambur (Jerusalem artichoke) (Helianthus tuberosus), to resist these conditions and degrade gluten. By 16S rDNA sequencing, we discovered that bacteria from the families Enterobacteriaceae, Bacillaceae, and Clostridiaceae most effectively multiply in conditions similar to the human GIT (microoxic conditions, 37 °C) while utilizing vegetable material and gluten as nutrients. Additionally, we used stomach simulation (1 h, pH 3) and intestinal simulation (1 h, bile salts 0.4%) treatments. The bacteria that survived this treatment retained the ability to degrade gluten epitopes but at lower levels. Four bacterial strains belonging to species Bacillus pumilus, Clostridium subterminale, and Clostridium sporogenes isolated from vegetable roots produced proteases with postproline cleaving activity that successfully neutralized the toxic immunogenic epitopes. Key points • Bacteria from root vegetables can degrade gluten. • Some of these bacteria can resist conditions mimicking gastrointestinal tract.

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“…Gluten-degrading peptidases are also found in organisms involved in the decomposition of organic matter. Family S28 prolyl endopeptidases from the fungus Aspergillus niger and edible mushroom in the family Physalacriaceae, Flammulina velutipes, are unique in the serine peptidase family because they have endopeptidase activity that cleaves after XP (Edens et al 2005;Stepniak et al 2006;Kang et al 2013;Schulz et al 2018). Aspergillus niger AN-PEP is active between a pH of 2 and 8, with an optimal activity between pH 4 and 5.…”

Section: Other Enzymes Of Nonhuman Originmentioning

confidence: 99%

Gluten-degrading bacteria: availability and applications

Kõiv

Tenson

2021

Appl Microbiol Biotechnol

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Gluten is a mixture of storage proteins in wheat and occurs in smaller amounts in other cereal grains. It provides favorable structure to bakery products but unfortunately causes disease conditions with increasing prevalence. In the human gastrointestinal tract, gluten is cleaved into proline and gluten rich peptides that are not degraded further. These peptides trigger immune responses that might lead to celiac disease, wheat allergy, and non-celiac gluten sensitivity. The main treatment option is a gluten-free diet. Alternatively, using enzymes or microorganisms with gluten-degrading properties might alleviate the disease. These components can be used during food production or could be introduced into the digestive tract as food supplements. In addition, natural food from the environment is known to enrich the microbial communities in gut and natural environmental microbial communities have high potential to degrade gluten. It remains to be investigated if food and environment-induced changes in the gut microbiome could contribute to the triggering of gluten-related diseases. Key points • Wheat proteins, gluten, are incompletely digested in human digestive tract leading to gluten intolerance. • The only efficient treatment of gluten intolerance is life-long gluten-free diet. • Environmental bacteria acquired together with food could be source of gluten-degrading bacteria detoxifying undigested gluten peptides.

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A prolyl endopeptidase from Flammulina velutipes for the possible degradation of celiac disease provoking toxic peptides in cereal proteins

Cited by 14 publications

References 35 publications

A DyP-Type Peroxidase of Pleurotus sapidus with Alkene Cleaving Activity

A DyP-Type Peroxidase of Pleurotus sapidus with Alkene Cleaving Activity

Microbiome of root vegetables—a source of gluten-degrading bacteria

Gluten-degrading bacteria: availability and applications

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