Pasta is a popular carbohydrate-based food with a low glycemic response. A continuous protein matrix which entraps starch granules and/or limits/retards starch hydrolysis by α-amylase is thought to be an important factor in explaining the slow digestion of starch in pasta. The characteristics of the protein matrix may also play an important role in determining the rate of starch digestion in pasta and therefore its glycemic response. In this study, the structural and physicochemical characteristics of the protein matrix of pasta were modified by varying the number of passes through sheeting rollers to investigate their effect on in vitro starch digestibility. The results show that the proteins dissociated from the starch granules with increasing sheeting passes thereby allowing an increased degree of digestion of starch.
Transglutaminase is a crosslinking enzyme that is finding increasing use in foods, yet the molecular changes responsible for its effects are not fully understood. Proteins were extracted from bread and croissant doughs that had been treated with transglutaminase and compared to those from control doughs by size exclusion high performance liquid chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. Transglutaminase increased the amount of protein extracted in the gliadin fraction in both bread and croissant doughs. In croissant doughs, a corresponding decrease in the protein extracted in the albumin to globulin fraction was seen. In each case, crosslinking of the high molecular weight glutenins was observed. The possible role of each of these changes on the functional properties of baked products is discussed.
BackgroundStarch is biosynthesised by a complex of enzymes including various starch synthases and starch branching and debranching enzymes, amongst others. The role of all these enzymes has been investigated using gene silencing or genetic knockouts, but there are few examples of overexpression due to the problems of either cloning large genomic fragments or the toxicity of functional cDNAs to bacteria during cloning. The aim of this study was to investigate the function of potato STARCH BRANCHING ENZYME II (SBEII) using overexpression in potato tubers.ResultsA hybrid SBEII intragene consisting of potato cDNA containing a fragment of potato genomic DNA that included a single intron was used in order to prevent bacterial translation during cloning. A population of 20 transgenic potato plants exhibiting SBEII overexpression was generated. Compared with wild-type, starch from these tubers possessed an increased degree of amylopectin branching, with more short chains of degree of polymerisation (DP) 6–12 and particularly of DP6. Transgenic lines expressing a GRANULE-BOUND STARCH SYNTHASE (GBSS) RNAi construct were also generated for comparison and exhibited post-transcriptional gene silencing of GBSS and reduced amylose content in the starch. Both transgenic modifications did not affect granule morphology but reduced starch peak viscosity. In starch from SBEII-overexpressing lines, the increased ratio of short to long amylopectin branches facilitated gelatinisation, which occurred at a reduced temperature (by up to 3°C) or lower urea concentration. In contrast, silencing of GBSS increased the gelatinisation temperature by 4°C, and starch required a higher urea concentration for gelatinisation. In lines with a range of SBEII overexpression, the magnitude of the increase in SBEII activity, reduction in onset of gelatinisation temperature and increase in starch swollen pellet volume were highly correlated, consistent with reports that starch swelling is greatly dependent upon the amylopectin branching pattern.ConclusionThis work reports the first time that overexpression of SBEII has been achieved in a non-cereal plant. The data show that overexpression of SBEII using a simple single-intron hybrid intragene is an effective way to modify potato starch physicochemical properties, and indicate that an increased ratio of short to long amylopectin branches produces commercially beneficial changes in starch properties such as reduced gelatinisation temperature, reduced viscosity and increased swelling volume.Electronic supplementary materialThe online version of this article (doi:10.1186/s12896-015-0143-y) contains supplementary material, which is available to authorized users.
Cereal Chem. 83(1):62-68Millstream flours, bran, pollard, and germ fractions were prepared from two Australian and two New Zealand wheat cultivars using a pilotscale roller mill. The distribution of six redox enzymes in milling fractions and the relationship of the enzymes to baking parameters were investigated. Lipoxygenase (LOX), dehydroascorbate reductase (DAR), and protein disulfide isomerase (PDI) tended to be higher in the tail-end fractions of break and reduction flour streams, but the highest levels were in the bran, pollard, and germ fractions. These enzymes had moderate to strong correlations with ash content of flour. These results indicated that a considerable amount of these enzymes in the tail-end flour streams were likely to be derived from contamination with bran, aleurone, or germ components of grain. Peroxidase (POX) tended to be higher in the break flours, but polyphenol oxidase (PPO) and ascorbate oxidase (AOX) tended to be evenly distributed in the millstream flours. These three enzymes generally had poor correlations with ash and baking parameters. LOX and DAR had a negative correlation with the baking quality of bread made in the absence of ascorbic acid (AA) but a poor correlation with improvement of bread quality made with AA. The negative correlation probably reflects the high content of ash (hence trichomes), glutathione, and protein thiols in those fractions that have high LOX and DAR, and these high-reducing-power components and trichomes in flour may be the actual cause of poor quality bread. PDI generally had a poor correlation with bread quality in the absence of AA but a significant positive correlation with improvement in the quality of bread made with AA. It thus seems that the endogenous levels of these six enzymes were not a limiting factor in the breadmaking process, except for PDI, the levels of which may have positively influenced breadmaking in the presence of AA.
Flour mill streams prepared from two Australian and two New Zealand wheat cultivars using a pilot‐scale roller mill were analyzed for rheological and baking quality characteristics and for protein composition using size‐exclusion HPLC. Differences in mill stream protein composition, on an industrially relevant scale, and the relationships between the distribution of proteins (and their degree of thiol exposure) and the technological quality of the flour mill streams were examined. Consistent, significant differences were observed in the physicochemical and processing characteristics of the flour streams. Between mill streams, changes in the quantities of the storage protein groups were more marked than for nonstorage protein groups. Changes in protein composition differed between the break and reduction stream flours. In contrast, the degree of exposure of thiol groups on the various protein groups followed different patterns between mill streams. Numerous significant relationships were observed between dough mixing and product baking tests and the composition and thiol exposure state of the various protein classes. These relationships are discussed in context of manipulating the processing quality of flour‐based products using mill streaming. A possible role for exposed thiol groups on storage proteins in the phenomenon of flour “aging” is suggested.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.