Effects of alpha-amylases from different sources on the firming of concentrated wheat starch gels: relationship to bread staling.
The firming and carbohydrate fractions of concentrated starch gels supplemented with four alpha-amylases from different sources were evaluated. Correlations were found between the firmness data and results for the carbohydrate fractions extracted from the gels. The thermostable (TBA) and intermediate temperature stability (ISBA) bacterial alpha-amylases were most effective in decreasing the rate of firming. The cereal alpha-amylase at the high level (CAH) was also effective. The CAH produced the largest quantity of dextrins at storage time zero and the thermostable bacterial alpha-amylase at the high level (TBAH) after storage for 5 days. None of the maltooligosaccharides appeared to be responsible for the decreased rate of firming of the gels. The results indicated that the TBA and ISBA most effectively inhibited firming because they degraded the external branches and the intercluster regions of amylopectin during storage. Consideration of previously reported differential scanning calorimetry and X-ray crystallography results leads to the conclusion that the antifirming action of the TBA and ISBA is due to their ability to degrade the amylopectin and amorphous regions of the gels during storage, which inhibits the formation of double helices and decreases the strength of the starch gel matrix. Gels supplemented with the TBA and ISBA were most crystalline but firmed to a lesser extent. These results are similar to those previously reported by other researchers for bread and strongly suggest that starch retrogradation plays a primary role in bread staling.
Palacios
Hernan R
HR
Department of Cereal and Food Sciences, North Dakota State University, Fargo, North Dakota 58105, USA.
Schwarz
Paul B
PB
D'Appolonia
Bert L
BL
D000687:Amylopectin / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology; D001939:Bread / Q000032:analysis*; D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D018360:Crystallography, X-Ray; D002523:Edible Grain / Q000201:enzymology; D004795:Enzyme Stability; D005519:Food Preservation; D005524:Food Technology; D005782:Gels / Q000737:chemistry / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D017433:Protein Structure, Secondary; D013213:Starch / Q000737:chemistry / Q000378:metabolism*; D014908:Triticum / Q000737:chemistry*; D000516:alpha-Amylases / Q000378:metabolism*
D005782:Gels; D013213:Starch; D000687:Amylopectin; D000516:alpha-Amylases