Crystal structure analysis of pyrrolidone carboxyl peptidase from Thermus thermophilus

Dhanalakshmi, K.; Kuramitsu, Seiki; Yokoyama, Shigeyuki; Kumarevel, Thirumananseri; Ponnuraj, Karthe

doi:10.1016/j.bpc.2022.106946

Cited by 2 publications

(1 citation statement)

References 21 publications

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“…Among them were a member of the S9 family of serine peptidases, prolyl oligopeptidase (POP) and pyrrolidone-carboxylate peptidase (Pcp), which were both identified only in L. casei LC130 and L. paracasei LPC100, but not in the inefficient gliadin scavenger, L. plantarum LP140. Of these two unique enzymes, Pcp is involved in the removal of L-pyroglutamic acid from the amino-terminus of pyroglutamyl proteins or peptides [35] and has never been shown to have a role in the hydrolysis of gliadins, while POP endopeptidase is considered a key microbial enzyme in the degradation of immunogenic peptides [36][37][38]. Among the enzymes that were encoded in higher copy numbers in L. casei LC130 and L. paracasei LPC100 compared to L. plantarum LP140 were two metalloendopeptidases PepO and PepF and proline iminopeptidase PepI.…”

Section: Discussionmentioning

confidence: 99%

Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases

Leszczyńska,

Szczepankowska,

Majak

et al. 2024

Nutrients

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Immunoreactive gluten peptides that are not digested by peptidases produced by humans can trigger celiac disease, allergy and non-celiac gluten hypersensitivity. The aim of this study was to evaluate the ability of selected probiotic strains to hydrolyze immunoreactive gliadin peptides and to identify peptidase-encoding genes in the genomes of the most efficient strains. Residual gliadin immunoreactivity was measured after one- or two-step hydrolysis using commercial enzymes and bacterial peptidase preparations by G12 and R5 immunoenzymatic assays. Peptidase preparations from Lacticaseibacillus casei LC130, Lacticaseibacillus paracasei LPC100 and Streptococcus thermophilus ST250 strains significantly reduced the immunoreactivity of gliadin peptides, including 33-mer, and this effect was markedly higher when a mixture of these strains was used. In silico genome analyses of L. casei LC130 and L. paracasei LPC100 revealed the presence of genes encoding peptidases with the potential to hydrolyze bonds in proline-rich peptides. This suggests that L. casei LC130, L. paracasei LPC100 and S. thermophilus ST250, especially when used as a mixture, have the ability to hydrolyze immunoreactive gliadin peptides and could be administered to patients on a restricted gluten-free diet to help treat gluten-related diseases.

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