Determination of molecular driving forces involved in heat-induced corn germ proteins gelation
文献类型: 外文期刊
作者: Sun, Xiang Dong 1 ; Lan, Yu 3 ; Shi, Dan 3 ; Lu, Shu Wen 2 ; Liao, Hui 1 ; Zhang, Rui Ying 1 ; Yao, Xin Miao 2 ; Zhang, Y 1 ;
作者机构: 1.Heilongjiang Acad Agr Sci, Qual & Safety Inst Agr Prod, Harbin 150086, Peoples R China
2.Heilongjiang Acad Agr Sci, Food Proc Inst, Harbin 150086, Peoples R China
3.East Univ Heilongjiang, Dept Food Sci, Harbin 150086, Peoples R China
关键词: Corn germ protein;Storage modulus;Molecular forces;Gelation;Reagents
期刊名称:JOURNAL OF CEREAL SCIENCE ( 影响因子:3.616; 五年影响因子:3.891 )
ISSN:
年卷期:
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收录情况: SCI
摘要: Molecular forces involved in corn germ proteins (CGP) gelation were investigated using a rheometer. With the inclusion of urea and guanidine hydrochloride (GuHCl), the storage moduli (G') of CGP gels tends to decrease. This is an indication that hydrophobic interactions and hydrogen bonds are present. The involvement of propylene glycol (PG) provides evidence that hydrogen bonds and electrostatic interactions are present. The impact of thiocyanate (NaSCN) and sodium sulfate (Na2SO4) further proves the involvement of hydrogen bonds. The effects of 2-mercaptoethanol (2-ME) and N-ethylmaleimide (NEM) reveal that involvement of disulfide bonds contribute to CGP gel stiffness. Reheating and recooling tests revealed that during the initial cooling phase the gel is thermally reversible and higher levels of G' suggested more hydrogen bonds are formed when recooled. It can be deduced that hydrogen bonds play a greater role than hydrophobic interactions from the increasing G' during cooling and recooling. (C) 2015 Elsevier Ltd. All rights reserved.
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