These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Effect of alpha-amylases from different sources on the retrogradation and recrystallization of concentrated wheat starch gels: relationship to bread staling. Author: Palacios HR, Schwarz PB, D'Appolonia BL. Journal: J Agric Food Chem; 2004 Sep 22; 52(19):5978-86. PubMed ID: 15366852. Abstract: Concentrated starch gels were supplemented with four alpha-amylases from different sources. The retrogradation and recrystallization of the gels were evaluated using differential scanning calorimetry (DSC) and X-ray crystallography. Correlations between the retrogradation data and the carbohydrate fractions extracted from these gels were determined. The thermostable (TBA) and intermediate temperature stability (ISBA) bacterial alpha-amylases were most effective in decreasing the rate of retrogradation of the starch in the gels. The cereal alpha-amylase at the high level (CAH) was also effective. Supplementation with the alpha-amylases increased the crystallinity of the gels. Gels supplemented with TBA or ISBA were most crystalline and retrograded to a lesser extent. The results indicated that DSC gives not only a measure of recrystallized amylopectin but also a measure of total order (recrystallized amylopectin and double-helical content). The maltooligosaccharides produced by the enzymes did not appear to be responsible for the reduced rates of retrogradation, but they appeared to be an expression of the degree of starch modification that was responsible for the inhibition of retrogradation. The crystallinity and retrogradation data were similar to results reported for bread and strongly suggest that bread staling is caused by the retrogradation of starch. The results also indicate that alpha-amylases decrease the rate and extent of retrogradation of starch gels by inhibiting the formation of double helices.[Abstract] [Full Text] [Related] [New Search]