Cloning and expression of synthetic genes encoding native, hybrid- and bacteriocin-derived chimeras from mature class IIa bacteriocins, by Pichia pastoris (syn. Komagataella spp.)

Arbulu, Sara; Jiménez, Juan J.; Gútiez, Loreto; Feito, Javier; Cintas, Luis M.; Herranz, Carmen; Hernández, Pablo E.

doi:10.1016/j.foodres.2019.01.015

Cited by 23 publications

(7 citation statements)

References 48 publications

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“…By contrast, rLactoliserin BU expressed in P. pastoris displayed a broad antibacterial spectrum. These results were in accordance with some recombinant peptides obtained from P. pastoris such as EntP::EntHF peptide [19], Hispidalin [18], Mytichitin-A [11], and defensins (including NZ2114 and its derivatives) [20].…”

Section: Antimicrobial Activitysupporting

confidence: 88%

Antimicrobial property of recombinant Lactolisterin BU in vitro and its initial application in pork refrigerated storage

et al. 2021

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Lactolisterin BU is a novel bacteriocin identified from Lactococcus lactis in 2017. It exhibits antimicrobial activity against food spoilage and foodborne pathogens. In this study, Lactolisterin BU was expressed in Pichia pastoris (P.pastoris) and isolated from the supernatant of yeast culture for the first time. It was found to exhibit a broad antimicrobial spectrum and rapid bactericidal activity against foodborne bacterial pathogens, both gram-positive and gram-negative ones, with minimum inhibition concentrations ranging within 10–60 μg/mL. The recombinant Lactolisterin BU (rLactolisterin BU) also had an antioxidant effect and was resistant to heating, acid–base, and high-dose-saline treatments and barely had any hemolytic activity or cytotoxicity. Moreover, rLactolisterin BU effectively suppressed the growth of bacterial pathogens; suppressed the increases in pH, total volatile basic nitrogen (TVB-N), and thiobarbituric acid reactive substances (TBARS) of pork samples; and maintained a high quality of fresh pork during storage at 4 ℃. Furthermore, rLactolisterin BU effectively inhibited the growth of three kinds of bacteria in a pork-spoilage model. Taken together, rLactolisterin BU could be a promising preservative for food storage.

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Section: Antimicrobial Activitysupporting

confidence: 88%

Antimicrobial property of recombinant Lactolisterin BU in vitro and its initial application in pork refrigerated storage

et al. 2021

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“…Three commonly used methods exist for the analysis of MS data. The first is the database search [ [151] , [156] , [168] ], which involves comparing theoretical enzyme digestion with theoretical fragments to identify peptides that match the MS spectrum. The identification information obtained through this method is derived from the sequences generated by known coding regions in the database.…”

Section: Discussionmentioning

confidence: 99%

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

Fang,

Yu,

et al. 2024

Heliyon

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“…Enterocin P was heterologously secreted and obtained better yield and biological activity in P. pastoris X‐33 (Gutierrez et al., 2005). In addition, enterocin HF and enterocin CRL35 expressed in P. pastoris X‐33 displayed antimicrobial activity (Arbulu et al., 2019). Besides, EntL50A and EntL50B, the leaderless two‐peptide bacteriocin produced by E. faecium L50, were efficiently expressed by MFα1s through the Sec system in yeast P. pastoris X‐33 (Basanta et al., 2010).…”

Section: Heterologous Expressionmentioning

confidence: 99%

Mining, heterologous expression, purification, antibactericidal mechanism, and application of bacteriocins: A review

Cui

Luo

Wang

et al. 2020

Comp Rev Food Sci Food Safe

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Bacteriocins are generally considered as low‐molecular‐weight ribosomal peptides or proteins synthesized by G+ and G− bacteria that inhibit or kill other related or unrelated microorganisms. However, low yield is an important factor restricting the application of bacteriocins. This paper reviews mining methods, heterologous expression in different systems, the purification technologies applied to bacteriocins, and identification methods, as well as the antibacterial mechanism and applications in three different food systems. Bioinformatics improves the efficiency of bacteriocins mining. Bacteriocins can be heterologously expressed in different expression systems (e.g., Escherichia coli, Lactobacillus, and yeast). Ammonium sulfate precipitation, dialysis membrane, pH‐mediated cell adsorption/desorption, solvent extraction, macroporous resin column, and chromatography are always used as purification methods for bacteriocins. The bacteriocins are identified through electrophoresis and mass spectrum. Cell envelope (e.g., cell permeabilization and pore formation) and inhibition of gene expression are common antibacterial mechanisms of bacteriocins. Bacteriocins can be added to protect meat products (e.g., beef and sausages), dairy products (e.g., cheese, milk, and yogurt), and vegetables and fruits (e.g., salad, apple juice, and soybean sprouts). The future research directions are also prospected.

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Cloning and expression of synthetic genes encoding native, hybrid- and bacteriocin-derived chimeras from mature class IIa bacteriocins, by Pichia pastoris (syn. Komagataella spp.)

Cited by 23 publications

References 48 publications

Antimicrobial property of recombinant Lactolisterin BU in vitro and its initial application in pork refrigerated storage

Antimicrobial property of recombinant Lactolisterin BU in vitro and its initial application in pork refrigerated storage

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

Mining, heterologous expression, purification, antibactericidal mechanism, and application of bacteriocins: A review

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