Analysis of nisin A, nisin Z and their degradation products by LCMS/MS

Schneider, Nadine; Werkmeister, K.; Pischetsrieder, Monika

doi:10.1016/j.foodchem.2011.01.023

Cited by 35 publications

(38 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In other words, 50 % of the initial amount of nisin was destroyed during the storage period. In general, the activity of nisin is known to decrease during food processing and storage because of the effects of temperature, pH, and components in the cheese matrix (Delves-Broughton 1990;Schneider et al 2011). Our results are consistent with previously reported results.…”

Section: Stability Of Nisin During Storage In a Refrigeratorsupporting

confidence: 93%

“…For the natural cheese, the CV for nisin A was less than 2.2 %, whereas that for nisin Z was less than 2.6 % ( Table 2). The present study confirmed that the method developed gave greatly improved recovery (80-113 %) and low CVs, for all types of cheese, compared with the recovery value (48-68 %) obtained from the study of Schneider et al (2011).…”

Section: Methods Validation and Cross-validationsupporting

confidence: 85%

“…As Schneider et al (2011) report an LC-MS/MS method for the simultaneous analysis of nisin A and nisin Z, we used identical MRM conditions to those used by Schneider et al (2011) for determining nisin A and nisin Z in cheese. However, as their pretreatment is so complex and needs long time, we developed a novel pretreatment to improve % recovery.…”

Section: Comparison With Other Studiesmentioning

confidence: 99%

“…As most of quantitative methods using LC-MS and liquid chromatography-tandem mass spectrometry (LC-MS/MS) on foodstuffs including cheese determine only nisin A, these methods are not available to detect nisin Z (Fuselli et al 2012;ISO 2009). To overcome such disadvantages, Schneider et al (2011) developed an LC-MS/MS method for the determination of nisin A, nisin Z, and their degradation products. However, further improvements to this method are needed due to low recovery.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Improved Pretreatment Method for Determination of Nisins A and Z and Monitoring in Cheese Using Liquid Chromatrography-Tandem Mass Spectrometry

Ko¹,

Park²,

Lim³

et al. 2015

Food Anal. Methods

View full text Add to dashboard Cite

The peptide nisin produced by Lactococcus lactis subsp. lactis is known to be one of the natural preservatives that are used in various foods including cheese products. This study optimized and validated a liquid chromatographytandem mass spectrometry method for determining nisin A and nisin Z in cheese. Processed and natural cheeses were used for method validation. In addition, this study investigated the content of nisin A and nisin Z in 140 cheese samples comprised of imported and domestic cheese. The nisin A and nisin Z contents of 140 cheese samples were determined. An extraction solution consisting of 0.1 M acetate buffer containing 1 M NaCl (pH 2.0) and methanol (NaCl/MeOH, 1:1v/ v) was the optimal solution for nisin extraction from cheese. The limits of quantification of nisin A and nisin Z were approximately 10.2 and 12.6 μg/kg, respectively. For processed cheese and natural cheese, the recoveries were 80.1-107.3 % for nisin A and 74.4-113.9 % for nisin Z and low coefficients of variation. In monitoring study, nisins A and Z were detected in only three soft processed cheese out of 140 samples. The proposed analysis procedure can be used as an efficient tool for determination of nisin A and nisin Z in cheese using liquid chromatography-tandem mass spectrometry (LC-MS/MS).

show abstract

Section: Stability Of Nisin During Storage In a Refrigeratorsupporting

confidence: 93%

Section: Methods Validation and Cross-validationsupporting

confidence: 85%

Section: Comparison With Other Studiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Improved Pretreatment Method for Determination of Nisins A and Z and Monitoring in Cheese Using Liquid Chromatrography-Tandem Mass Spectrometry

Ko¹,

Park²,

Lim³

et al. 2015

Food Anal. Methods

View full text Add to dashboard Cite

show abstract

“…In this respect, it has been reported that Met in bacteriocins become spontaneously oxidized, especially during their purification to homogeneity, leading to a loss or reduction in their antimicrobial activity [64,65]. Moreover, the oxidation of thioether bridges and methionine residues has been described as a common modification of heat-treated or stored NisA and NisZ [66]. Interestingly, the bacteriocin activity quantified in the last RP-FPLC fraction represented a 179 % of the antimicrobial activity found in the culture supernatant and a 71,300-fold increase in the specific antimicrobial activity, which suggests that the oxidation events cited above may take place during the subsequent treatment of the purified bacteriocin for MALDI-TOF MS analysis.…”

Section: Discussionmentioning

confidence: 99%

Safety assessment, genetic relatedness and bacteriocin activity of potential probiotic Lactococcus lactis strains from rainbow trout (Oncorhynchus mykiss, Walbaum) and rearing environment

Araújo

Muñoz-Atienza

Ramirez

et al. 2015

Eur Food Res Technol

View full text Add to dashboard Cite

in three well-defined and highly divergent groups (31.0 % similarity). Nine (12 %) L. lactis strains were identified as bacteriocin producers. The bacteriocin produced by L. lactis subsp. cremoris WA2-67 was purified, and mass spectrometry and DNA sequencing revealed its identity to nisin Z (NisZ). Altogether, the results allowed the identification of 34 (45.3 %) putatively safe lactococci, including three bacteriocinogenic strains. This is the first description of tet(K), tet(O) and tet(T) in L. lactis. Moreover, ERIC-PCR fingerprinting has been shown for the first time as a valuable tool for genetic profiling of L. lactis strains from aquatic origin. A NisZ-producing L. lactis strain has been isolated for the first time from an aquatic environment, and this strain may be considered as a potential probiotic for rainbow trout farming for improving the quality and safety of fish and fish products.

show abstract

A Cell‐Free Platform Based on Nisin Biosynthesis for Discovering Novel Lanthipeptides and Guiding their Overproduction In Vivo

et al. 2020

View full text Add to dashboard Cite

Lanthipeptides have extensive therapeutic and industrial applications. However, because many are bactericidal, traditional in vivo platforms are limited in their capacity to discover and mass produce novel lanthipeptides as bacterial organisms are often critical components in these systems. Herein, the development of a cell‐free protein synthesis (CFPS) platform that enables rapid genome mining, screening, and guided overproduction of lanthipeptides in vivo is described. For proof‐of‐concept studies, a type I lanthipeptide, nisin, is selected. Four novel lanthipeptides with antibacterial activity are identified among all nisin analogs in the National Center for Biotechnology Information (NCBI) database in a single day. Further, the CFPS platform is coupled with a screening assay for anti‐gram‐negative bacteria growth, resulting in the identification of a potent nisin mutant, M5. The titers of nisin and the nisin analog are found to be improved with CFPS platform guidance. Owing to the similarities in biosynthesis, the CFPS platform is broadly applicable to other lanthipeptides, thereby providing a universal method for lanthipeptide discovery and overproduction.

show abstract

Analysis of nisin A, nisin Z and their degradation products by LCMS/MS

Cited by 35 publications

References 24 publications

Improved Pretreatment Method for Determination of Nisins A and Z and Monitoring in Cheese Using Liquid Chromatrography-Tandem Mass Spectrometry

Improved Pretreatment Method for Determination of Nisins A and Z and Monitoring in Cheese Using Liquid Chromatrography-Tandem Mass Spectrometry

Safety assessment, genetic relatedness and bacteriocin activity of potential probiotic Lactococcus lactis strains from rainbow trout (Oncorhynchus mykiss, Walbaum) and rearing environment

A Cell‐Free Platform Based on Nisin Biosynthesis for Discovering Novel Lanthipeptides and Guiding their Overproduction In Vivo

Contact Info

Product

Resources

About