Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters










Database
Language
Publication year range
1.
J Agric Food Chem ; 63(16): 4196-201, 2015 Apr 29.
Article in English | MEDLINE | ID: mdl-25843595

ABSTRACT

Maltogenic α-amylase is widely used as an antistaling agent in bakery foods. The objective of this study was to determine the degree of hydrolysis (DH) and starch structure after maltogenic amylase treatments in relation to its retrogradation. Waxy maize starch was cooked and hydrolyzed to different degrees by a maltogenic amylase. High-performance anion-exchange chromatography and size exclusion chromatography were used to determine saccharides formed and the molecular weight (Mw) distributions of the residual starch structure, respectively. Chain length (CL) distributions of debranched starch samples were further related to amylopectin (AP) retrogradation. Differential scanning calorimetry (DSC) results showed the complete inhibition of retrogradation when starches were hydrolyzed to >20% DH. Mw and CL distributions of residual AP structure indicated that with an increase in %DH, a higher proportion of unit chains with degree of polymerization (DP) ≤9 and a lower proportion of unit chains with DP ≥17 were formed. A higher proportion of short outer AP chains that cannot participate in the formation of double helices supports the decrease in and eventual inhibition of retrogradation observed with the increase in %DH. These results suggest that the maltogenic amylase could play a powerful role in inhibiting the staling of baked products even at limited starch hydrolysis.


Subject(s)
Amylopectin/chemistry , Zea mays/chemistry , alpha-Amylases/chemistry , Calorimetry, Differential Scanning , Hydrolysis , Molecular Weight
2.
J Agric Food Chem ; 62(40): 9819-31, 2014 Oct 08.
Article in English | MEDLINE | ID: mdl-25177767

ABSTRACT

Grain protein composition determines quality traits, such as value for food, feedstock, and biomaterials uses. The major storage proteins in sorghum are the prolamins, known as kafirins. Located primarily on the periphery of the protein bodies surrounding starch, cysteine-rich ß- and γ-kafirins may limit enzymatic access to internally positioned α-kafirins and starch. An integrated approach was used to characterize sorghum with allelic variation at the kafirin loci to determine the effects of this genetic diversity on protein expression. Reversed-phase high performance liquid chromatography and lab-on-a-chip analysis showed reductions in alcohol-soluble protein in ß-kafirin null lines. Gel-based separation and liquid chromatography-tandem mass spectrometry identified a range of redox active proteins affecting storage protein biochemistry. Thioredoxin, involved in the processing of proteins at germination, has reported impacts on grain digestibility and was differentially expressed across genotypes. Thus, redox states of endosperm proteins, of which kafirins are a subset, could affect quality traits in addition to the expression of proteins.


Subject(s)
Endosperm/chemistry , Plant Proteins/analysis , Sorghum/chemistry , Chromatography, High Pressure Liquid/methods , Electrophoresis, Polyacrylamide Gel , Genotype , Glutaredoxins/metabolism , Lab-On-A-Chip Devices , Mutation , Phylogeny , Plant Proteins/genetics , Plant Proteins/metabolism , Prolamins/metabolism , Proteomics , Seed Storage Proteins/metabolism , Sorghum/genetics , Tandem Mass Spectrometry , Thioredoxins/metabolism
3.
Food Chem ; 153: 193-9, 2014 Jun 15.
Article in English | MEDLINE | ID: mdl-24491720

ABSTRACT

Octenylsuccinic anhydride (OSA)-modified starches with a low (0.018) and high (0.092) degree of substitution (DS) were prepared from granular native waxy maize starch in aqueous slurry. The position of OS substituents along the starch chains was investigated by enzyme hydrolysis followed by chromatographic analysis. Native starch and two OS starches with a low and high DS had ß-limit values of 55.9%, 52.8%, and 34.4%, respectively. The weight-average molecular weight of the ß-limit dextrin from the OS starch with a low DS was close to that of the ß-limit dextrin from native starch but lower than that of the ß-limit dextrin from the OS starch with a high DS. Debranching of OS starches was incomplete compared with native starch. OS groups in the OS starch with a low DS were located on the repeat units near the branching points, whereas the OS substituents in the OS starch with a high DS occurred both near the branching points and the non-reducing ends.


Subject(s)
Starch/analogs & derivatives , Zea mays/chemistry , Hydrolysis , Molecular Structure , Oxidation-Reduction , Starch/chemistry , Viscosity
4.
J Agric Food Chem ; 61(18): 4448-54, 2013 May 08.
Article in English | MEDLINE | ID: mdl-23581620

ABSTRACT

The purpose of this study was to investigate the effects of tannins on starch digestion in tannin-containing sorghum extracts and wholegrain flours from 12 sorghum varieties. Extracts reduced amylase activity in a tannin concentration-dependent manner when the extract was mixed with the enzyme before substrate (amylopectin) addition, with higher molecular weight tannins showing greater reduction. Conversely, when the extract and substrate were combined before enzyme addition an enhancement in amylase activity was experienced. In uncooked, cooked, and cooked and stored wholegrain sorghum flours, rapidly digestible, slowly digestible, and resistant starches were not correlated with tannin content or molecular weight distribution. Resistant starch increased from 6.5% to 22-26% when tannins were added to starch up to 50% (starch weight). Tannin extracts both reduced and enhanced amylase activity depending on conditions, and, while these trends were clear in extracts, the effects on starch digestion in wholegrain flours was more complex.


Subject(s)
Flour/analysis , Sorghum/chemistry , Starch/chemistry , Tannins/chemistry , alpha-Amylases/metabolism , Amylopectin/chemistry , Catechin/chemistry , Cellulose/chemistry , Cooking , Food Handling/methods , Molecular Weight , Plant Extracts/chemistry
5.
J Sci Food Agric ; 93(5): 1233-41, 2013 Mar 30.
Article in English | MEDLINE | ID: mdl-23011944

ABSTRACT

BACKGROUND: Tannins are large polyphenolic polymers and are known to bind proteins, limiting their digestibility, but are also excellent antioxidants. Numerous studies investigating the functional properties of sorghum tannin have been conducted by comparing grain samples from different sorghum lines without considering the other intrinsic characteristics of the grain. The purpose of this study was to remove the confounding intrinsic factors present in the endosperm so the effect of the tannins could be evaluated utilizing a unique decortication/reconstitution procedure. RESULTS: The tannin content of the 14 cultivars tested ranged from 2.3 to 67.2 catechin equivalents. The bran fractions were studied for their impact on protein binding and antioxidant capacity. Protein digestibility by pepsin ranged from 8% to 58% at the highest tannin level addition. Protein binding ranged from 3.11 to 16.33 g blue bovine serum albumin kg⁻¹ bran. Antioxidant capacity ranged from 81.33 to 1122.54 µmol Trolox equivalents g⁻¹ bran. High-performance size-exclusion chromatography detailed molecular size distributions of the tannin polymers and relationship to tannin functionality. CONCLUSION: The tannin content and composition play a significant role in determining tannin functionality. These differences will allow for selections of high-tannin sorghums with consideration of the biological activities of the tannins.


Subject(s)
Antioxidants/analysis , Crops, Agricultural/chemistry , Flour/analysis , Seeds/chemistry , Sorghum/chemistry , Tannins/analysis , Antimetabolites/analysis , Antimetabolites/chemistry , Antimetabolites/metabolism , Antioxidants/chemistry , Antioxidants/metabolism , Chemical Phenomena , Crops, Agricultural/growth & development , Crops, Agricultural/metabolism , Dietary Carbohydrates/analysis , Dietary Carbohydrates/metabolism , Dietary Proteins/metabolism , Digestion , Endosperm/chemistry , Endosperm/growth & development , Endosperm/metabolism , Kansas , Mechanical Phenomena , Molecular Weight , Pepsin A/antagonists & inhibitors , Pepsin A/metabolism , Plant Proteins/metabolism , Proteolysis , Seeds/growth & development , Seeds/metabolism , Sorghum/growth & development , Sorghum/metabolism , Species Specificity , Surface Properties , Tannins/chemistry , Tannins/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL
...