2006
DOI: 10.1016/j.foodchem.2005.03.038
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Freezing of soybeans influences the hydrophobicity of soy protein

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Cited by 20 publications
(10 citation statements)
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“…When the pre-treatment by freezing was performed ( Figure 1, F), the cracking of the structure was observed due to freezing effects. During the freezing of the fluid (water), the crystals formed fill a greater volume inside the tissue, so that, when thawed, the spaces occupied by the ice crystals are free observing the cracking of the structure [24,25]. The same effects on rice husk structure after freezing was reported by Chang, Thitikorn-amorn [9].On the other hand, alkaline pretreatment with 8% NaOH (Figure 1, A) caused erosion in the structure.…”
Section: Effect Of Pre-treatments On Rice Husk Microstructuresupporting
confidence: 56%
“…When the pre-treatment by freezing was performed ( Figure 1, F), the cracking of the structure was observed due to freezing effects. During the freezing of the fluid (water), the crystals formed fill a greater volume inside the tissue, so that, when thawed, the spaces occupied by the ice crystals are free observing the cracking of the structure [24,25]. The same effects on rice husk structure after freezing was reported by Chang, Thitikorn-amorn [9].On the other hand, alkaline pretreatment with 8% NaOH (Figure 1, A) caused erosion in the structure.…”
Section: Effect Of Pre-treatments On Rice Husk Microstructuresupporting
confidence: 56%
“…This sample exhibited very low values of ΔH and PS (<70%), indicating that 7S and 11S globulins were partially denatured and aggregated. These results can be understood if one considers that the freezing of soybeans produces an increase in the surface hydrophobicity of proteins, which favors protein aggregation (20).…”
Section: Resultsmentioning
confidence: 99%
“…Furthermore, both dynamic moduli were higher in the FM samples than in the F/TM ones (Table 2). It has been reported that freeze treatment increased the hydrophobicity of soy protein regardless of the heating treatment (Noh, Kang, Hong, & Yun, 2006). Because electrostatic interactions are one of the major forces maintaining protein tertiary and quaternary structures, an abrupt increase in ionic strength or salt concentration in the nonfrozen phase can cause competition with existing electrostatic bonds, which in turn leads to extensive aggregation of the protein structure (Xiong, 1997).…”
Section: Effect Of Spi Concentration and Freeze/thaw Cycle On Viscoelmentioning
confidence: 99%