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Characterisation of antibacterial peptide fractions extracted from pomelo nucleus co‐incubated with Lactobacillus
International Journal of Food Science & Technology ( IF 2.6 ) Pub Date : 2020-01-03 , DOI: 10.1111/ijfs.14473
Huifan Liu 1 , Geyi Wu 1 , Haifeng Song 1 , Huanyou Zhang 1 , Lukai Ma 1 , Charles Brennan 2 , Sufen Li 1 , Yingjun Liu 1 , Jihong Wu 3 , Qin Wang 1
Affiliation  

Pomelo have been widely reported for its unique flavour and high nutritive value, whereas the antibacterial activity of pomelo nucleus peptides was still poorly understood. We characterised a co‐incubation system of pomelo nucleus and Lactobacillus amylolyticus L6 to identify peptides of high application value. We first analysed the structure of pomelo nucleus peptides (GP) and co‐incubated peptides (C‐GP) by scanning electron microscopy, high‐performance gel permeation chromatography, liquid chromatography–tandem mass spectrometry and amino acid analysis. The results showed that the molecular weights, 89% of peptide sequences, and amino acid composition were different in the C‐GP compared with the GP fraction, and the spatial structures were quite diverse; the C‐GP peptide fraction presented irregular, amorphous and interwoven flocs. Notably, only C‐GP had antimicrobial activity against Escherichia coli (minimum inhibitory concentration of 12.50 μg/mL). Further assessment of the mechanism suggested that the hydrophobic groups in the C‐GP peptide fraction were inserted into the hydrophilic sites on the surface of the E. coli cell membrane, leading to the formation of holes and bending. These findings suggest the potential value of pomelo nucleus as a nutrient source.

中文翻译:

从与乳杆菌共孵育的柚核提取的抗菌肽级分的表征

柚子因其独特的风味和高营养价值而被广泛报道,而柚核肽的抗菌活性仍知之甚少。我们表征了柚核和解淀粉乳杆菌的共培养系统L6鉴定具有高应用价值的肽。我们首先通过扫描电子显微镜,高效凝胶渗透色谱,液相色谱-串联质谱和氨基酸分析来分析柚核肽(GP)和共孵育肽(C-GP)的结构。结果表明,与GP组分相比,C-GP的分子量,89%的肽序列和氨基酸组成均不同,并且空间结构差异很大。C-GP肽级分呈现不规则,无定形和交织的絮状物。值得注意的是,只有C-GP对大肠杆菌具有抗菌活性(最低抑制浓度为12.50μg/ mL)。对该机理的进一步评估表明,C-GP肽级分中的疏水基团被插入大肠杆菌细胞膜表面的亲水位点,导致孔的形成和弯曲。这些发现表明柚核作为营养源的潜在价值。
更新日期:2020-01-03
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