2016
DOI: 10.1007/s12539-016-0206-3
|View full text |Cite
|
Sign up to set email alerts
|

Change in Glutenin Macropolymer Secondary Structure in Wheat Sourdough Fermentation by FTIR

Abstract: Wheat sourdough was prepared by fermentation with Lactobacillus plantarum M616 and yeast in the present study. The change in secondary structure of glutenin macropolymer (GMP) in wheat sourdough fermentation for 4 and 12 h was determined using Fourier transform infrared spectroscopy, and then the resultant spectra were Fourier self-deconvoluted of the amide I band in the region from 1600 to 1700 cm. Significant different spectra especially in the amide I band for GMP from sourdough fermented with L. plantarum … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
8
0

Year Published

2020
2020
2024
2024

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 18 publications
(8 citation statements)
references
References 33 publications
0
8
0
Order By: Relevance
“…Attention should be paid to the changes in disulfide bond content during cross-linking, which determines the morphology of the protein [29]. The improvement in the rheological properties of the steamed bread and the reduction in its hardness were mainly due to the depolymerization of glutenin macromolecules, which made the cross-linking structure uniform and regular [30]. During proofing, hydrogen peroxide produced by L. plantarum promoted the oxidation of free sulfhydryl groups to form disulfide bonds and linked the hydrophobic amino acids in the molecule.…”
Section: Extractability Of Gluten Proteinmentioning
confidence: 99%
“…Attention should be paid to the changes in disulfide bond content during cross-linking, which determines the morphology of the protein [29]. The improvement in the rheological properties of the steamed bread and the reduction in its hardness were mainly due to the depolymerization of glutenin macromolecules, which made the cross-linking structure uniform and regular [30]. During proofing, hydrogen peroxide produced by L. plantarum promoted the oxidation of free sulfhydryl groups to form disulfide bonds and linked the hydrophobic amino acids in the molecule.…”
Section: Extractability Of Gluten Proteinmentioning
confidence: 99%
“…7a, the 1600–1700cm −1 band (amide I region) was selected for fitting analysis of the protein’s secondary structure (Wang et al . 2017; Wang et al . 2018).…”
Section: Resultsmentioning
confidence: 99%
“…After GOx was encapsulated, the asymmetric vibration peaks of the phosphate group were slightly shifted from 1088 to 1082 cm −1 , and the movement of these characteristic peaks proved the successful preparation of the integrated catalyst. 29,31,35 The surface composition of Fe 3 O 4 @Cu/GMP−GOx was characterized by X-ray photoelectron spectroscopy (XPS). As can be seen from Figure S3, C, N, O, P, and Cu could be observed in the analysis of Fe 3 O 4 @Cu/GMP−GOx, which was consistent with the results of EDX.…”
Section: Methodsmentioning
confidence: 99%