2023
DOI: 10.1007/s11694-023-02080-7
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Functionality of Barley pasta supplemented with Mungbean flour: cooking behavior, quality characteristics and morphological interactions

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Cited by 8 publications
(6 citation statements)
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“…The slightly variable bands at 1653 cm –1 reflect CO vibration associated with amide-I bonds. The peaks positioned at 1551 cm –1 are associated with N–H bending and C–N stretching in relation to amide-II bonds of proteins . The peaks located at 1351 cm –1 reflect the C–H vibration .…”
Section: Resultsmentioning
confidence: 99%
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“…The slightly variable bands at 1653 cm –1 reflect CO vibration associated with amide-I bonds. The peaks positioned at 1551 cm –1 are associated with N–H bending and C–N stretching in relation to amide-II bonds of proteins . The peaks located at 1351 cm –1 reflect the C–H vibration .…”
Section: Resultsmentioning
confidence: 99%
“…The peaks positioned at 1551 cm −1 are associated with N−H bending and C−N stretching in relation to amide-II bonds of proteins. 54 The peaks located at 1351 cm −1 reflect the C−H vibration. 55 The band at around 2669 cm −1 was assigned to C−H stretching, and the intensity of this band was increased in the treated samples, and a more progressive increase was noticed in blanched and alkali-treated samples.…”
Section: ■ Results and Discussionmentioning
confidence: 99%
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“…The loss of solids is an indicator of pasta quality, considering it as the resistance to disintegration by cooking in water [30]. In a good quality pasta, the loss of solids due to cooking should be less than 10% [26].…”
Section: Effect Of Replacing Wf With Sprouted Pseudocereal and Cushur...mentioning
confidence: 99%
“…The amide I region in protein is around wavenumber 1632 cm À1 and amide II region around 1513 cm À1 and various carbohydrate features are between 1100 and 950 cm À1 (Garcia-Valle et al, 2021). The amide I zone, represented by the sharp peaks at 1636 cm À1 , depicts the strong vibration mode as a result of C=O stretching, which is crucial for revealing and analysing the protein's secondary structure (Singh et al, 2023b). The deformation of N-H occurred at a wavenumber range of 1660-1200 cm À1 expressing gelatin fractions.…”
Section: Ftir Spectramentioning
confidence: 99%