دورية أكاديمية

Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing.

التفاصيل البيبلوغرافية
العنوان: Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing.
المؤلفون: Wang, Xiaolong1,2 (AUTHOR), Appels, Rudi1,3 (AUTHOR) rudi.appels@unimelb.edu.au, Zhang, Xiaoke4 (AUTHOR), Bekes, Ferenc5 (AUTHOR), Diepeveen, Dean2,6 (AUTHOR), Ma, Wujun2 (AUTHOR), Hu, Xinzhong1 (AUTHOR), Islam, Shahidul1,2 (AUTHOR) S.Islam@murdoch.edu.au
المصدر: Food Chemistry. May2020, Vol. 312, pN.PAG-N.PAG. 1p.
مصطلحات موضوعية: *GLIADINS, *GEL electrophoresis, *WHEAT proteins, *HIGH performance liquid chromatography, *SOLUBILITY, *EXTRACELLULAR matrix proteins
مستخلص: • Binding strength of dough protein is showed by its solubility in a set of buffers. • Starch pasting causes overall solubility loss of total protein in dough matrix. • Gliadins and some metabolic proteins are released from dough matrix after heating. • A response to extraction-system is developed for tracking protein behavior. To understand wheat dough protein behavior under dual mixing and thermal treatment, solubility of Mixolab-dough proteins were investigated using nine extraction buffers of different dissociation capacities. Size exclusion high performance liquid chromatography (SE-HPLC) and two-dimensional gel electrophoresis (2-DGE) demonstrated that overall changes of protein fractions and dynamic responses of specific proteins during dough processing were well reflected by their solubility variations. After starch pasting, the abundance of 0.5 M NaCl extractable proteins were decreased except for six protein groups including α-amylase inhibitors and superoxide dismutase (SOD). The solubility loss of glutenin proteins at C3 (32 min; 80 ℃) was mainly ascribed to the un-extractable HMW-GSs, LMW-GSs, globulin and triticin, while the extract yield of α-, β-, γ-gliadins and avenin-like proteins (ALPs) increased after starch pasting. Differential responses of dough proteins to extraction systems provides the basis for further exploring wheat protein dynamics in processing. [ABSTRACT FROM AUTHOR]
قاعدة البيانات: Academic Search Index
الوصف
تدمد:03088146
DOI:10.1016/j.foodchem.2019.126038