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Effects of Sulfur-Containing Amino Acids and High Hydrostatic Pressure on Structure and Gelation Properties of Sweet Potato Protein

文献类型: 外文期刊

作者: Zhao, Zhong-Kai 1 ; Mu, Tai-Hua 1 ; Zhang, Miao 1 ; Richel, Aurore 2 ;

作者机构: 1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Lab Food Chem & Nutr Sci, Minist Agr & Rural Affairs,Key Lab Agroprod Proc, 2 Yuan Ming Yuan West Rd,POB 5109, Beijing 100193, Peoples R China

2.Univ Liege, Lab Biomass & Green Technol, Gembloux Agrobio Tech, Passage Deportes 2, B-5030 Gembloux, Belgium

关键词: Sweet potato protein; High hydrostatic pressure; Sulfur-containing amino acids; Gelation; Low-field NMR

期刊名称:FOOD AND BIOPROCESS TECHNOLOGY ( 影响因子:4.465; 五年影响因子:4.793 )

ISSN: 1935-5130

年卷期: 2019 年 12 卷 11 期

页码:

收录情况: SCI

摘要: The structural modification and gelation properties of sweet potato protein (SPP) affected by sulfur-containing amino acids (L-cysteine or L-cystine) and high hydrostatic pressure (HHP) were investigated. Additives altered the denaturation temperature and reduced the denaturation enthalpy of SPP. Higher alpha-helical contents were observed in untreated or HHP-treated SPP with L-cysteine or L-cystine, while beta-sheet and random coil structure unit were decreased. FTIR spectra showed a weak absorbance in HHP-treated SPP with L-cysteine and L-cystine. Storage modulus (G ') of untreated or HHP-treated SPP was enhanced by L-cysteine and L-cystine. Textural properties of SPP gels were improved by sulfur-containing amino acids and HHP, especially for L-cysteine. Decrease in T-2b relaxation time and increase in A(21) proportion peak area by low-field NMR suggested that water bound more closely to SPP molecules in the presence of L-cysteine and L-cystine, and more immobilized water fraction was trapped in SPP gel matrix.

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