Enzyme-aided investigation of the substituent distribution in cationic potato amylopectin starch.
The distribution of substituents along the polymer chain in cationic potato amylopectin starch, modified in solution, granular slurry, or dry state, was investigated. The starch derivatives were successively hydrolyzed by different enzymes, followed by characterization of the hydrolysis products obtained by means of electrospray mass spectrometry (ESI-MS) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). ESI-MS and MALDI-MS were proved to be appropriate techniques for identification of the substituted hydrolysis products, for which there are no standard compounds available. No highly substituted oligomers were found in the hydrolysates, which was taken as an indication of a more or less homogeneous distribution of cationic groups in the amylopectin molecules. Furthermore, from the results obtained it was suggested that the enzymes cleave glucosidic linkages only between unsubstituted glucose units and, preferentially, linkages in sequences containing more than two adjacent unsubstituted units. The determination of the amount of unsubstituted glucose produced from every successive hydrolysis step revealed slight differences between the different starch samples with respect to the homogeneity of the substitution pattern. Among the three samples under investigation, starch cationized in solution was found to have the most and dry-cationized starch the least homogeneous distribution of substituents.
Richardson
Sara
S
Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
Nilsson
Gunilla
G
Cohen
Arieh
A
Momcilovic
Dane
D
Brinkmalm
Gunnar
G
Gorton
Lo
L
D000687:Amylopectin / Q000032:analysis* / Q000378:metabolism; D002412:Cations; D006868:Hydrolysis; D011198:Solanum tuberosum / Q000201:enzymology*; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods
D002412:Cations; D000687:Amylopectin