A study on the functional properties of taro starches from Tonga : a thesis presented in partial fulfilment of the requirements for the degree of Master of Technology in Food Technology at Massey University

This study compared the functional properties of three taro starches extracted from selected cultivars, one from each of the three most commonly grown taro genera in Tonga. The selected cultivars were Alocasia macrorrhiza var 'Fohenga', Colocasia esculenta var 'Lau'ila', and Xanthosoma saggitifolium var 'Mahele'uli'. Cassava starch, a commercial product from Thailand, was studied together with the taro starches for comparison purposes. Freshly harvested taro corms/cormels were peeled, washed, ground into pulp. The taro pulp was washed with excess water and filtered with a cheese cloth. The solid pulp was discarded, and the water-starch mixture (starch milk) was collected in a settling tank. The starch was held for 10-24 hours to allow the starch to settle, and then the supernatant liquid was discarded. The Xanthosoma starch was successfully isolated using this method. For the Alocasia and Colocasia, the starch could not be isolated from the starch milk due to the presence of a mucilaginous material, and it was separated using a bowl centrifuge. The starches were dried, in a hot-air drier and then purified to remove trace of protein, fat, and fibre. All the taro starch granules were similarly polygonal in shape but the granule sizes were different. The Xanthosoma starch granule size (5-30μm) was similar to that of cassava starch granules (5-35μm). The granule sizes of Alocasia (0.5-3μm) and Colocasia (0.5-6μm) were very small, smaller than rice starch granules. The amylose contents, determined using an iodometric blue value colorimetry method, were 12.1, 13.6, 19.8, and 27.4% for Alocasia, Colocasia, cassava, and Xanthosoma starches respectively. The gelatinization temperatures for the starches were determined using sensory evaluation, hot stage microscopy, Brabender Amylograph, and Differential Scanning Calorimetry (DSC) methods. The gelatinization temperatures were approximately 69, 70, 75 and 80°C for cassava, Alocasia, Xanthosoma and Colocasia starches respectively. The gelatinization temperature ranges for Xanthosoma and Colocasia were similar to that of cassava starch, but Alocasia starch showed relatively wider temperature range. The viscosity of the Xanthosoma gelatinized starch paste was much higher than the other starches but showed greater breakdown on heating. The strengths of the starch gels were determined by measuring the rheological modulus G* of the gels using a Bohlin Rheometer, and the penetration strength test using an Instron. Both tests showed that the Xanthosoma starch produced a much stronger and higher viscosity gel than all of the cassava, Alocasia and Colocasia starches which produced gels with similar strength. The relative order of gel clarity from qualitative sensory evaluation, from highest to poorest clarity, was cassava, Xanthosoma, Colocasia, then Alocasia. The storage stability of the starch gels was evaluated by studying the crystallisation using DSC, and measuring the syneresis occurring during storage at 5 and 22°C. The Xanthosoma starch gel was extremely susceptible to crystallisation and syneresis during storage, compared with cassava, Colocasia, and Alocasia gels which had similar stabilities on storage. The freeze-thaw stability of the starch gels was studied by subjecting the starch gels to repeated freeze-thaw cycles. The Xanthosoma starch gel was extremely unstable with freeze-thaw treatment. The Alocasia and Colocasia starch gels were similar to cassava starch gel which was more stable with freeze-thaw treatment. The Xanthosoma starch, because of extremely high viscosity and gel strength, could be used in food products that need high viscous texture but require no further storage. The Colocasia and Alocasia starches, because of high digestibility due to very small granule sizes can be used in baby food formulations, which are either heat treated or frozen

NZNO Conference: ‘Look for potential in everyone’

Republished with the permission of the Kai Tiaki Editors

Институциональные условия усиления внедрения инвестиций интенсивного типа

Большое значение в процессе повышения эффективности общественного воспроизводства на основе усиления внедрения инноваций и инвестиций интенсивного типа имеет создание оптимальных институциональных условий и предпосылок. В этой связи в работе исследуются факторы формирования оптимальной институциональной среды как основы интенсификации российской экономики.Велике значення у процесі підвищення ефективності суспільного відтворення на основі посилення впровадження інновацій та інвестицій інтенсивного типу має створення оптимальних інституційних умов і передумов. У зв'язку із цим у роботі досліджуються чинники формування оптимального інституційного середовища як основи інтенсифікації російської економіки.Creation of optimal institutional conditions and preconditions is of great importance in the process of increasing the efficiency of public reproduction on the basis of strengthening the introduction of innovations and investments of intensive type. In this respect the factors of formation of optimal institutional environment as the bases for intensification of the Russian economy are analyzed

Studies on heat-induced interactions and gelation of whey protein : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Food Technology

The purpose of this study was to gain greater understanding of the interactions of whey proteins during heat-induced gelation of whey protein concentrate (WPC) solutions. Attention was focused on gaining better knowledge of the relationship between composition of WPC and its ability to form heat-induced gels, and to explore the mechanisms of protein aggregation and gelation in WPC solutions. Interactions of whey proteins (β-lactalbumin, α-lactalbumin and BSA) were studied in three types of commercial WPC (rennet, cheese and acid) solutions, as well as in pure protein model systems, using one-dimensional (1D-) and two-dimensional (2D-) polyacrylamide gel electrophoresis (PAGE), size exclusion chromatography, light scattering and ultracentrifugation. The formation and structure of aggregates and gels were determined by oscillatory rheometry, confocal scanning laser microscopy (CSLM) and transmission electron microscopy (TEM) techniques. Examination of heated (75 °C) rennet WPC solutions at a range of concentrations (10-120 g/kg, pH 6.8) revealed that the extent of protein aggregation and the formation of the intermediate molecular weight products were concentration-dependent. The rates of loss of β-lactoglobulin, α-lactalbumin and BSA during heating increased as the WPC concentration was increased from 10 to 120 g/kg. 2D-PAGE showed that some disulphide-linked β-lactoglobulin dimers were present in heated 10 g/kg solution, but very little was present in heated 120 g/kg solution. SDS was able to dissociate monomeric protein from high molecular weight aggregates in heated 120 g/kg WPC solution but not in 10 g/kg WPC solution. This suggested that in addition to disulphide-linked aggregates, hydrophobic aggregates involving β-lactoglobulin, α-lactalbumin and BSA were formed in heated WPC solutions at high protein concentrations. Examination of the heated acid WPC and cheese WPC solutions (120 g/Kg), using 1D-PAGE and size exclusion chromatography, revealed that the loss of β-lactoglobulin, α-lactalbumin and BSA from the cheese WPC solution was faster than the loss of the same proteins from the acid WPC solutions. It was also found that a considerable proportion of aggregates formed in heated cheese WPC solution was linked by hydrophobic association, whereas the aggregates formed in heated acid WPC solutions were linked predominantly by disulphide bonds. TEM and CLSM showed that the aggregates formed in cheese WPC solution were relatively large and "particulated," whereas the aggregates formed in acid WPC solution were small and "fine stranded." The gels formed from the heated cheese WPC solutions had low gel strength and high syneresis, whereas the gels obtained from the acid WPC had high gel strength and good water holding capacity. Results of the dialysis experiments revealed that the differences between the properties of the acid WPC and the cheese WPC gels could be explained largely by their different mineral compositions. Relatively higher concentrations of divalent cations, Ca and Mg, in the cheese WPC was considered to be responsible for high rates of loss of native-like proteins, and the formation of large, hydrophobically-associated and "particulated" aggregates. High concentrations of monovalent cation in the acid WPC solutions probably resulted in slower loss native-like proteins and formation of small and 'fine-stranded" aggregates. Attempt was made to characterise the nature of "insoluble" material in the unheated acid and cheese WPC solutions. Although, both the acid and the cheese WPC solutions contained considerable amounts of "insoluble" material, the amounts in the cheese WPC were greater. This material contained disproportionately higher levels of aggregated BSA and the minor whey proteins; in the cheese WPC it also contained considerable amounts of aggregated β-lactoglobulin and α-lactalbumin as well as phospholipids. The "insoluble" material in acid WPC, had higher casein content. The presence of this material did not appear to affect the gelation characteristics of the cheese WPCs, but had a positive effect on acid WPC gelation. Studies on model systems of pure proteins showed that β-lactoglobulin, α-lactalbumin and BSA interacted to form homogeneous aggregates of each other as well as heterogeneous aggregates. 2D-PAGE clearly showed that when a mixture of these proteins was heated, initially BSA formed aggregates with itself and β-lactoglobulin and α-lactalbumin formed co-aggregates at a later stage of heating. Based on these results, the structure of WPC gel was suggested to be a heterogeneous network formed largely by co-polymers of β-lactoglobulin and α-lactalbumin embedded with "clusters" or "strands" of BSA aggregates. Based on the results of this study, recommendations are made on how this information can be used in the development of new or improved whey products

Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment

Bovine b-lactoglobulin (b-lg), a-lactalbumin (a-la) and bovine serum albumin (BSA), dispersed in ultra®ltration permeate, that had been prepared from whey protein concentrate solution (100 g}kg, pH 6±8), were heated at 75 °C. The consequent protein aggregation was studied by one-dimensional (1D) and twodimensional (2D) polyacrylamide gel electrophoresis (PAGE). When 100 g b-lg}kg permeate solution was heated at 75 °C, cooled and examined, large aggregates were observed. These aggregates were partially dissociated in SDS solution to give monomers, disulphide-bonded dimers, trimers and larger aggregates. When mixtures of b-lg and a-la or BSA were heated, homopolymers of each protein as well as heteropolymers of these proteins were observed. These polymer species were also observed in a heated mixture of the three proteins. Two-dimensional PAGE of mixtures demonstrated that these polymers species contained disulphide-bonded dimers of b-lg, a-la and BSA, and 1:1 disulphide-bonded adducts of a-la and b-lg, or BSA. These results are consistent with a mechanism in which the free thiols of heattreated b-lg or BSA catalyse the formation of a range of monomers, dimers and higher polymers of a-la. It is likely that when whey protein concentrate is heated under the present conditions, BSA forms disulphide-bonded strands ahead of b-lg and that a-la aggregation with b-lg and with itself is catalysed by the heat-induced unfolded BSA and b-lg

Effect of adding low levels of β-mercaptoethanol on the disulphide bonds of κ-casein and β-lactoglobulin solutions

Low levels of b-mercaptoethanol (up to 0.5%, v/v) were added to k-casein and b-lactoglobulin solutions (5 mg mL 1), mixtures thereof, and milk. The reduction of disulphide bonds was monitored over time for up to 24 h, using micro-fluidic electrophoresis, at temperatures ranging from 20 to 50 C. Lower concentrations of b-mercaptoethanol and a shorter reaction time were required to reduce k-casein to the same extent as b-lactoglobulin. This suggests that the intermolecular disulphide bonds of k-casein were more accessible than the intra-molecular disulphide bonds of b-lactoglobulin. The reduction of b-lactoglobulin at any b-mercaptoethanol concentration and reaction time was enhanced as the temperature increased up to 50 C. The level of reduced k-casein increased with increasing temperature during the first 2 h; however, as the reaction time was prolonged, the level of monomeric k-casein decreased. This suggests that monomeric k-casein can re-form disulphide bonds via either re-oxidation or thiol-disulphide exchange reactions