♥ welcome
♥ about the bread
Created: 10 April 2010Leader: Lynnette Heng
Members: Lorelle Ang
Soh Chin Yi
Goh Ai Ting
Li Yuen Ying
♥SIP placements
Lynnette: KK Hospital- DietitianChin Yi: Gardenia- R&D
Ai Ting: Singapore Sports Council- Nutritionist
Yuen Ying: KH Roberts- lab assistant
Lorelle: OSIP (China)
Bread Staling
Monday, May 3, 2010
Bread staling is increased by transglutaminase(TG) addition. Martin, Zeleznak,
and Hoseney (1991) suggested that interactions between the swollen starch granules and the protein network actively contribute to crumb firming. Upon analysis of bread crumb, significant differences in starch–protein matrix have been detected in the course of storage (Blaszczak et al., 2004). TG-induced strengthening effect could increase such interactions and favour bread staling and simultaneous crumb elasticity preservation during storage. The affinity to water promoted by TG in gluten (Gerrard et al., 1998) could also limit the water availability for starch and accelerate its retrogradation. On the contrary, alpha-amylase (AMYL), xylanase (XYL) and protease (PROT) exhibited a significant antistaling effect. PROT showed the most marked effect on reducing hardness, which came accompanied by a significant slowing down in gumminess and chewiness evolution in the time. According with the conclusions of Armero and Collar (1998), crumb firming during storage mainly depends on initial crumb firmness. Through studies carried out on model systems, Rojas, Rosell, and Benedito de Barber (2001) concluded that maltodextrins were responsible for the antistaling effect promoted by addition of a-amylase to bread formulation. They proposed the existence of a mechanism of partial obstruction of starch retrogradation. Jimenez and Martınez-Anaya (2001) proved that water-insoluble pentosans (WIP) were positively correlated with crumb elasticity and hardness during storage. Similarly, the improvement of bread shelf-life through PROT addition possibly would be tied with the increase of the water available for starch, in conjunction with a simultaneous diminution of starch–protein interactions as consequence of the hydrolysis of peptide bonds in the protein molecules. Babiker, Fujisawa, Matsudomi, and Kato (1996) previously reported an increase in the hydrophobicity of protease-treated gluten. Statistical analysis of the textural data during storage proved significant.
and Hoseney (1991) suggested that interactions between the swollen starch granules and the protein network actively contribute to crumb firming. Upon analysis of bread crumb, significant differences in starch–protein matrix have been detected in the course of storage (Blaszczak et al., 2004). TG-induced strengthening effect could increase such interactions and favour bread staling and simultaneous crumb elasticity preservation during storage. The affinity to water promoted by TG in gluten (Gerrard et al., 1998) could also limit the water availability for starch and accelerate its retrogradation. On the contrary, alpha-amylase (AMYL), xylanase (XYL) and protease (PROT) exhibited a significant antistaling effect. PROT showed the most marked effect on reducing hardness, which came accompanied by a significant slowing down in gumminess and chewiness evolution in the time. According with the conclusions of Armero and Collar (1998), crumb firming during storage mainly depends on initial crumb firmness. Through studies carried out on model systems, Rojas, Rosell, and Benedito de Barber (2001) concluded that maltodextrins were responsible for the antistaling effect promoted by addition of a-amylase to bread formulation. They proposed the existence of a mechanism of partial obstruction of starch retrogradation. Jimenez and Martınez-Anaya (2001) proved that water-insoluble pentosans (WIP) were positively correlated with crumb elasticity and hardness during storage. Similarly, the improvement of bread shelf-life through PROT addition possibly would be tied with the increase of the water available for starch, in conjunction with a simultaneous diminution of starch–protein interactions as consequence of the hydrolysis of peptide bonds in the protein molecules. Babiker, Fujisawa, Matsudomi, and Kato (1996) previously reported an increase in the hydrophobicity of protease-treated gluten. Statistical analysis of the textural data during storage proved significant.
- P.A. Caballero, M.Gomez,C.M. Rosell (n.d) website: http://www.aseanfood.info/Articles/11019317.pdf retrieved on 26th april 2010