Publication no. C-2004-0202-02R |  VIEW ARTICLE

Using Visible and Near-Infrared Reflectance Spectroscopy and Differential Scanning Calorimetry to Study Starch, Protein, and Temperature Effects on Bread Staling.

Feng Xie (1), Floyd E. Dowell (2,3), and Xiuzhi S. Sun (1). (1) Department of Grain Science and Industry, 201 Shellenberger, Kansas State University, Manhattan, KS 66506. (2) USDA-ARS, Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502. (3) Corresponding author. Phone: 785-776-2753. Fax: 785-537-5550. E-mail: <fdowell@gmprc.ksu.edu> Cereal Chem. 81(2):249-254. Accepted September 8, 2003. This article is in the public domain and not copyrightable. It may be freely reprinted with customary crediting of the source. American Association of Cereal Chemists, Inc., 2004.

Starch, protein, and temperature effects on bread staling were investigated using visible and near-infrared spectroscopy (NIRS) and differential scanning calorimetry (DSC). Bread staling was mainly due to amylopectin retrogradation. NIRS measured amylopectin retrogradation accurately in different batches. Three important wavelengths, 970 nm, 1,155 nm, and 1,395 nm, were associated with amylopectin retrogradation. NIRS followed moisture and starch structure changes when amylopectin retrograded. The amylose-lipid complex changed little from one day after baking. The capability of NIRS to measure changes in the retrograded amylose-lipid complex was limited. Two important wavelengths, 550 nm and 1,465 nm, were key for NIRS to successfully classify the starch-starch (SS) and starch-protein (SP) bread based on different colors and protein contents in SS and SP. Low temperature dramatically accelerated the amylopectin retrogradation process. Protein retarded bread staling, but not as much as temperature. The starch and protein interaction was less important than the starch retrogradation. Protein hindered the bread staling process mainly by diluting starch and retarding starch retrogradation.