2016
DOI: 10.1007/s10853-016-0336-3
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Preparation, characterization and antifungal properties of polysaccharide–polysaccharide and polysaccharide–protein films

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Cited by 25 publications
(16 citation statements)
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“…At the wavenumbers range from 1,700 to 800 cm −1 , three samples (MSC0, MSC0.6, MSC1.2) presented different characteristics. As displayed in Figure 4, for MSC0, signals at wavenumbers of 1,153, 1,040, and 925 cm −1 were mainly caused by glycosyl bond vibrations and CO stretching of polysaccharides, which were typical bands corresponding to MBS and SSPSs (Castaño et al, 2017; Tao, Zhang, & Yu, 2007). With the incorporation of nano‐emulsified CCO, the peak around 2,880 cm −1 became stronger, relating to the CH stretching (CH 2 ) of the CCO.…”
Section: Resultsmentioning
confidence: 99%
“…At the wavenumbers range from 1,700 to 800 cm −1 , three samples (MSC0, MSC0.6, MSC1.2) presented different characteristics. As displayed in Figure 4, for MSC0, signals at wavenumbers of 1,153, 1,040, and 925 cm −1 were mainly caused by glycosyl bond vibrations and CO stretching of polysaccharides, which were typical bands corresponding to MBS and SSPSs (Castaño et al, 2017; Tao, Zhang, & Yu, 2007). With the incorporation of nano‐emulsified CCO, the peak around 2,880 cm −1 became stronger, relating to the CH stretching (CH 2 ) of the CCO.…”
Section: Resultsmentioning
confidence: 99%
“…Generally, the blue shift of amides I and II indicates a more ordered conformation strengthened by hydrogen bonds in the protein/κ-C system. 10,37 The new band of 1160 cm −1 in SMGHs/κ-C and SMGHs/DNase/κ-C was considered as a glycoside bond, owing to the binding of κ-C. 38 This new peak also appears at 1157 cm −1 in fava bean protein/κ-C, suggesting that signals around 1150 cm −1 are attributed to vibrations of the glycosidic linkage of the polysaccharides. 38 Furthermore, it was necessary to note the blue shift of sulfate groups in κ-C (1263 cm −1 ), which was observed in SMGHs/κ-C and SMGHs/DNase/κ-C at 1237 cm −1 .…”
Section: Resultsmentioning
confidence: 99%
“…10,37 The new band of 1160 cm −1 in SMGHs/κ-C and SMGHs/DNase/κ-C was considered as a glycoside bond, owing to the binding of κ-C. 38 This new peak also appears at 1157 cm −1 in fava bean protein/κ-C, suggesting that signals around 1150 cm −1 are attributed to vibrations of the glycosidic linkage of the polysaccharides. 38 Furthermore, it was necessary to note the blue shift of sulfate groups in κ-C (1263 cm −1 ), which was observed in SMGHs/κ-C and SMGHs/DNase/κ-C at 1237 cm −1 . We hypothesized that the blue shift of sulfate groups might be due to the loss of one oxygen group during charge interactions between SMGHs and κ-C, because Sonawane et al 37 have discussed that SO of sulfate ester of κ-C shifts from 1261 to 1213 cm −1 when gelatin binds to κ-C, resulting from the loss of one oxygen through electrostatic interaction.…”
Section: Resultsmentioning
confidence: 99%
“…To be specific, 6 distinct zones were monitored. For the peaks that correspond to the ANS conformational changes, the peaks are 950 cm -1 , 1000 cm -1 , and 2890 cm -1 which attributed to starch 1,4-glycosidic linkages, the C-O-C bond of glucopyranose ring and C-H bond of starch aliphatic chain respectively [24][25][26][27]. For XNBR conformational changes, peaks at cm -1 , cm -1 , and 1549 cm -1 were observed.…”
Section: Morphological Analysismentioning
confidence: 99%