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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 Sci Food Agric ; 94(10): 2133-6, 2014 Aug.
Article in English | MEDLINE | ID: mdl-24343522

ABSTRACT

BACKGROUND: The HCI-vanillin assay is a well-accepted method for determining tannin content in sorghum but is limited to small sample sets due to the time-consuming nature of the method. The objective was to develop an accurate and repeatable high-throughput 96-well plate assay for breeders to screen large sample sets of sorghum for tannin content. Validation of the high-throughput assay was tested on 25 sorghums suspected to contain tannin. RESULTS: Approximately 30 measurements per day were completed using the conventional assay compared to 224 measurements using the 96-well platform. The correlation between the two tannin assays was 0.98. The coefficient of variation (CV) was 3.54% and 3.21% for the 96-well and conventional method, respectively. The 96-well assay exhibited good repeatability, with the inter-plate CV between 2.77% and 4.85%. CONCLUSION: The high-throughput 96-well HCI-vanillin assay exhibited an eightfold increase in the number of measurements completed and was as accurate as the conventional HCI-vanillin assay.


Subject(s)
Benzaldehydes/analysis , Edible Grain/chemistry , High-Throughput Screening Assays/methods , Sorghum/chemistry , Tannins/analysis , High-Throughput Screening Assays/standards , Humans , Reproducibility of Results , Seeds/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
6.
J Invertebr Pathol ; 105(1): 112-5, 2010 Sep.
Article in English | MEDLINE | ID: mdl-20460127

ABSTRACT

A microsporidium that closely resembles Paranosema species at the level of the light microscope was isolated from the rusty grain beetle, Cryptolestes ferrugineus. It's identity as Nosema oryzaephili (originally described from Oryzaephilus surinamensis) was confirmed by comparison with a known isolate of N. oryzaephili based on spore size, small subunit rDNA sequence, and relative infectivity to O. surinamensis, Tribolium castaneum, and Ephestia kuehniella. Phylogenetic analysis of the small subunit rDNA indicates clearly that this species belongs in the genus Paranosema and thus the designation Paranosema oryzaephili (Burges, Canning and Hurst) is proposed. In spite of the abundance, economic importance, and world-wide distribution of C. ferrugineus, this is the first report of a microsporidial infection in this species. This is also the first report of P. oryzaephili in the new world.


Subject(s)
Coleoptera/microbiology , Nosema/genetics , Nosema/isolation & purification , Phylogeny , Animals , DNA, Fungal/genetics , DNA, Ribosomal/genetics , Microsporidia, Unclassified/isolation & purification , Microsporidia, Unclassified/pathogenicity , Microsporidiosis/microbiology , Nosema/pathogenicity
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