Cloning, Expression, and Chromosomal Stabilization of thePropionibacterium shermaniiProline Iminopeptidase Gene (pip) for Food-Grade Application inLactococcus lactis

Leenhouts, Kees; Bolhuis, Albert; Boot, J. H.; Deutz, Inge; Toonen, Marjolein Y.; Venema, Gerard; Kok, Jan; Ledeboer, A.M.

doi:10.1128/aem.64.12.4736-4742.1998

Cited by 28 publications

(10 citation statements)

References 49 publications

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“…The corresponding functions were proposed as new annotation for their four CDS, [see Additional file 1 ] for all new annotations. PF#1882 is a previously characterised proline iminopeptidase of P. freudenreichii [EMBL: AJ001361 ] [ 39 ] and PF#61 is a paralogous of PF#1882 in P. freudenreichii CIP103027 T . PF#435 possess all the sequence characteristics of prolyl oligopeptidases (peptidase family S9) [ 40 ].…”

Section: Resultsmentioning

confidence: 99%

A genomic search approach to identify esterases in Propionibacterium freudenreichii involved in the formation of flavour in Emmental cheese

Dherbécourt¹,

Falentin²,

Canaan

et al. 2008

Microb Cell Fact

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Background: Lipolysis is an important process of cheese ripening that contributes to the formation of flavour. Propionibacterium freudenreichii is the main agent of lipolysis in Emmental cheese; however, the enzymes involved produced by this species have not yet been identified. Lipolysis is performed by esterases (carboxylic ester hydrolases, EC 3.1.1.-) which are able to hydrolyse acylglycerols bearing short, medium and long chain fatty acids. The genome sequence of P. freudenreichii type strain CIP103027 T was recently obtained in our laboratory.

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Section: Resultsmentioning

confidence: 99%

A genomic search approach to identify esterases in Propionibacterium freudenreichii involved in the formation of flavour in Emmental cheese

Dherbécourt¹,

Falentin²,

Canaan

et al. 2008

Microb Cell Fact

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“…It specifically catalyses the removal of the N‐terminal proline residue from peptides or proteins (Cunningham and O'Connor, ), and can also remove N‐terminal l ‐alanine or d ‐alanine from substrates, albeit at lower efficiency (Alonso and Garcia, ). In the food industry, PIP is used to debitterize the peptides in cheese processing (Leenhouts et al ., ; Tan et al ., ) and in the synthesis of proline‐containing dipeptides (Yamamoto et al ., ). These studies have elaborated the biochemical properties and biotechnological applications of PIP.…”

Section: Introductionmentioning

confidence: 98%

A dual role for proline iminopeptidase in the regulation of bacterial motility and host immunity

Kan

et al. 2018

Molecular Plant Pathology

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During plant-pathogen interactions, pathogenic bacteria have evolved multiple strategies to cope with the sophisticated defence systems of host plants. Proline iminopeptidase (PIP) is essential to Xanthomonas campestris pv. campestris (Xcc) virulence, and is conserved in many plant-associated bacteria, but its pathogenic mechanism remains unclear. In this study, we found that disruption of pip in Xcc enhanced its flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xcc restricted its bacterial motility by elevating c-di-GMP levels. We also found that PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not host plants. When we transformed pip into the host plant Arabidopsis, higher bacterial titres were observed in pip-overexpressing plants relative to wild-type plants after Xcc inoculation. The repressive function of PIP on plant immunity was dependent on PIP's enzymatic activity and acted through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. Both processes provide bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants.

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“…The gene coding PepI in propionibacteria was cloned and multiplied in the chromosome of Lc. lactis (Leenhouts et al . 1998).…”

Section: Enzymes From Microorganisms That Are Important For Cheese Rimentioning

confidence: 99%

Dairy enzymology

Stepaniak

2004

Int J of Dairy Tech

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The properties and the significance of the principal indigenous enzymes in milk, milk coagulants, enzymes from dairy microorganisms participating in cheese ripening, and spoilage enzymes are discussed. In particular, the properties of plasmin, lipases, phosphatases, enzymes from somatic cells, enzymes involved in antimicrobial and antiviral systems in milk, enzymes from lactic acid bacteria, propionibacteria, and microorganisms involved in smear‐ and mould‐ripened cheese are reviewed. Some assay methods and the impact of some processing factors on selected enzymes are also discussed.

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Cloning, Expression, and Chromosomal Stabilization of thePropionibacterium shermaniiProline Iminopeptidase Gene (pip) for Food-Grade Application inLactococcus lactis

Cited by 28 publications

References 49 publications

A genomic search approach to identify esterases in Propionibacterium freudenreichii involved in the formation of flavour in Emmental cheese

A genomic search approach to identify esterases in Propionibacterium freudenreichii involved in the formation of flavour in Emmental cheese

A dual role for proline iminopeptidase in the regulation of bacterial motility and host immunity

Dairy enzymology

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