Design of bovine lactoferricin-derived peptide and its expression and activity in Pichia pastoris

Wang, Liang; Wang, Yulian; Zili, Lv; Enpeng, Zhang; Guo, Aizhen

doi:10.1016/j.bbrc.2020.10.098

Cited by 6 publications

(3 citation statements)

References 14 publications

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“…These data also corroborate the high purity of the rhLF and a lack of host protein presence. Interestingly, one peptide survived pepsin digestion with an approximate molecular weight of 2-3 kDa (Figure 2D) which correlates with published literature as lactoferricin, 51 and remains intact throughout the entire 60-minute exposure (Supplemental Figure 2E). Additionally, quantification of intact proteins shows similar amounts between rhLF and hmLF throughout the digestion procedure with no intact protein remaining by 10 minutes for rhLF and 20 minutes for hmLF (Figure 2E).…”

Section: Resultssupporting

confidence: 85%

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Evaluation of the potential food allergy risks of recombinant human lactoferrin expressed inKomagataella phaffii

Anaya,

Rosario Martinez,

Goodman

et al. 2024

Preprint

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Prior to the introduction of novel food ingredients into the food supply, safety risk assessments are required, and numerous prediction models have been developed and validated to evaluate safety. The allergenic risk potential of Helaina recombinant human lactoferrin (rhLF, Effera™), produced inKomagataella phaffii(K. phaffii) was assessed by literature search, bioinformatics sequence comparisons to known allergens, glycan allergenicity assessment, and a simulated pepsin digestion model. The literature search identified no allergenic risk for Helaina rhLF,K. phaffii, or its glycans. Bioinformatics search strategies showed no significant risk for cross-reactivity or allergenicity between rhLF or the 36 residual host proteins and known human allergens. Helaina rhLF was also rapidly digested in simulated gastric fluid and its digestibility profile was comparable to human milk lactoferrin (hmLF), further demonstrating a low allergenic risk and similarity to the hmLF protein. Collectively, these results demonstrate a low allergenic risk potential of Helaina rhLF and do not indicate the need for further clinical testing or serum IgE binding to evaluate Helaina rhLF for risk of food allergy prior to introduction into the food supply.

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Section: Resultssupporting

confidence: 85%

“…Interestingly, digested products (Helaina rhLF and hmLF) contained a small peptide that survived the entire digestion procedure, which corresponds in molecular weight to lactoferricin, a known peptide of lactoferrin. 51…”

Section: Discussionmentioning

confidence: 99%

Evaluation of the potential food allergy risks of recombinant human lactoferrin expressed inKomagataella phaffii

Anaya,

Rosario Martinez,

Goodman

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

“…Accordingly, P. pastoris aroused our interest because yeast could produce large amounts of functional recombinant proteins and perform many eukaryotic post-translational modifications, including protein folding and glycation, and the DNA manipulation, transformation and identification were easily to be achieved [11,12]. Moreover, many AMPs including bovine lactoferricin peptide [16], Microcin J25 [17], Mytichitin-A [11], Hispidalin [18], and mytichitin-CB [8], have been successfully expressed in P. pastoris and exhibited potent antimicrobial activity and high yields. In a previous study, Lactolisterin BU has been purified by reversed-phase high-performance liquid chromatography, but the production rate is unclear [10].…”

Section: Expression and Purification Of Rlactolisterin Bu From P Pastorismentioning

confidence: 99%

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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Expression and antimicrobial activity of the recombinant bovine lactoferricin in Pichia pastoris

Lv,

Zhang,

Wang

et al. 2024

Synthetic and Systems Biotechnology

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Design of bovine lactoferricin-derived peptide and its expression and activity in Pichia pastoris

Cited by 6 publications

References 14 publications

Evaluation of the potential food allergy risks of recombinant human lactoferrin expressed inKomagataella phaffii

Evaluation of the potential food allergy risks of recombinant human lactoferrin expressed inKomagataella phaffii

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

Expression and antimicrobial activity of the recombinant bovine lactoferricin in Pichia pastoris

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