Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate

Gelation characteristics of tropical surimi under water bath and ohmic heating

“…Heating rate in such a production line is about 100e120 C min À1 (Park, 2005), which is markedly higher than the heating rate applied to water bath heating for surimi gel quality testing. Heating rate is known to have a great effect on gelation of muscle proteins (Arntfield & Murray, 1992; Barbut & Mittal, 1990;Cofrades, Carballo, & JimCnezColmenero, 1997;Sun & Arntfield, 2011). A method to evaluate gel quality and provide information relevant to gel formation at the production line is therefore necessary for better quality control.…”

Effect of cooling–heating rate on sol-gel transformation of fish gelatin–gum arabic complex coacervate phase

“…Cooling or heating rate is important processing parameter which can be controlled to control gel formation in biopolymeric solutions by affecting on thermal history of the system [8]. The effect of cooling and heating rate on gelation of different proteins have been reported: β-lactoglobulin [9,4], whey protein [10], salt-extracted pea protein isolate [8], pea legumin [11].…”

“…Cooling or heating rate is important processing parameter which can be controlled to control gel formation in biopolymeric solutions by affecting on thermal history of the system [8]. The effect of cooling and heating rate on gelation of different proteins have been reported: β-lactoglobulin [9,4], whey protein [10], salt-extracted pea protein isolate [8], pea legumin [11]. It has demonstrated that at slower heating rate there is more time for protein denaturation and then, aggregation of the unfolded protein molecules through intermolecular hydrophobic interactions which eventually, caused to onset of gelation at a lower temperature and improvement of rheological properties of the gel [4,8,10].…”

“…The effect of cooling and heating rate on gelation of different proteins have been reported: β-lactoglobulin [9,4], whey protein [10], salt-extracted pea protein isolate [8], pea legumin [11]. It has demonstrated that at slower heating rate there is more time for protein denaturation and then, aggregation of the unfolded protein molecules through intermolecular hydrophobic interactions which eventually, caused to onset of gelation at a lower temperature and improvement of rheological properties of the gel [4,8,10]. Sun and Arntfield [8] and O'Kane et al [11] considered effect of cooling rate on network development and strength of the gel proteins.…”

“…It has demonstrated that at slower heating rate there is more time for protein denaturation and then, aggregation of the unfolded protein molecules through intermolecular hydrophobic interactions which eventually, caused to onset of gelation at a lower temperature and improvement of rheological properties of the gel [4,8,10]. Sun and Arntfield [8] and O'Kane et al [11] considered effect of cooling rate on network development and strength of the gel proteins. They found that stronger gels with more developed network structure can be formed at slower cooling rates because there is a longer time for optimal arrangement of unfolded proteins and formation of hydrogen bindings, as favorable bindings at low temperatures.…”