Factors affecting short-term and long-term stabilities of proteins

Arakawa, Tsutomu; Prestrelski, Steven J.; Kenney, William C.; Carpenter, John F.

doi:10.1016/0169-409x(93)90003-m

Cited by 233 publications

(165 citation statements)

References 88 publications

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“…Therefore, proteins must be stabilized against both of these fundamentally different stresses (Crowe et al 1990;. Lyoprotectants including saccharides, amino acids and sugar alcohols are used to stabilise the proteins during the freeze drying process (Arakawa et al 2001;Carvajal et al 2005;Shaviklo et al 2011aShaviklo et al , 2012Huda et al 2012).…”

Section: Freeze Dryingmentioning

confidence: 99%

Development of fish protein powder as an ingredient for food applications: a review

Shaviklo¹

2013

J Food Sci Technol

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The increasing awareness that dried fish protein can be applied for food fortification and production of value added/functional foods has encouraged the food industry to examine different methods for developing fish protein ingredient from different raw materials. Fish protein powder (FPP) is a dried and stable fish product, intended for human consumption, in which the protein is more concentrated than in the original fish flesh. Quality and acceptability of FPP depend on several factors. The fat content of the FPP is a critical issue because when it is oxidized a strong and often rancid flavour is produced. Protein content of FPP depends on the raw materials, amount of additives and moisture content, but it contains at least 65 % proteins. FPP is used in the food industry for developing re-structured and ready-to-eat food products. The FPP maintains its properties for 6 months at 5°C but loses them rapidly at 30°C. Deterioration of the FPP during storage is prevented by lowering the moisture content of the product and eliminating of oxygen from the package. The FPP can be applied as a functional ingredient for developing formulated ready-to-eat products. This article reviews methods for extracting fish proteins, drying methods, characteristics and applications of FPP and factors affecting FPP quality.

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Section: Freeze Dryingmentioning

confidence: 99%

Development of fish protein powder as an ingredient for food applications: a review

Shaviklo¹

2013

J Food Sci Technol

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“…Costantino et al [6] showed that interaction between proteins and lactose modify lactose crystallization kinetics. In addition, lactose is known to have an efficient cryo-protector due to lactose-protein hydrogen bonds, which could also act to reduce crystallization kinetics [1].…”

Section: Introductionmentioning

confidence: 99%

Study of lactose / β-lactoglobulin interactions during storage

Thomas

Scher

Desobry

2005

Lait

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-The objective of this study was to evaluate the interactions between lactose and β-lactoglobulin in β-lactoglobulin/lactose powders (BL powders) during storage. Model BL powders were produced by co-lyophilization of lactose with increasing quantities of β-lactoglobulin. Lyophilization produced lactose in the amorphous state, which is highly reactive and likely leads to agglomeration of industrial whey powders. The BL powders were stored at 20 ± 1 °C from 0.11 to 0.95 a w and their water sorption behaviour was studied gravimetrically. Before storage, BL powders were amorphous. After storage at high a w , a loss of water was observed on the moisture sorption isotherms of BL powders due to lactose crystals formation, detected by DSC and SEM analysis, and to the structural collapse of the powders. Lactose crystallization occurred at a w = 0.43 in pure lactose samples and at a w = 0.59 in BL powders containing 40% β-lactoglobulin. Moreover, β-lactoglobulin was responsible for a delayed crystallization process in BL powders. Thus, the water sorption behaviour of BL powders was very different from the behaviour of the two compounds mixed after separate lyophilization (B+L powders). These results pointed out interactions between lactose and β-lactoglobulin, which occurred during the lyophilization process and storage. Lactose/β-lactoglobulin interactions stabilized the BL powders against lactose crystallization. In the last part of the work, the nature of the interactions (covalent links, H bonds and hydrophobic links) and the kinetic aspect of the crystallization were studied. whey powder / lactose / β-lactoglobulin / interaction / storage Résumé -Étude des interactions lactose/β-lactoglobuline lors de la conservation. Les poudres obtenues à partir de lactosérum sont très souvent utilisées comme ingrédients alimentaires car elles possèdent d'intéressantes propriétés fonctionnelles (moussantes, gélifiantes…). Lors de la conservation de ces poudres, de nombreuses dégradations biologiques et physico-chimiques altèrent les propriétés fonctionnelles des produits, ainsi que les propriétés physiques et l'aspect des poudres (écoulement, couleur…). La stabilité de ces poudres dépend également fortement de la température de conservation ainsi que de l'activité de l'eau (a w ) et de la composition des produits. Des poudres modèles ont été préparées par co-lyophilisation de lactose avec des quantités croissantes (10 à 40 %) de β-lactoglobuline (poudres BL). Les poudres ont été conservées 3 mois à 20 ± 1 °C, à des activités de l'eau comprises entre 0,11 et 0,95. L'objectif de notre étude a été d'évaluer la présence ou l'absence d'interactions entre lactose et β-lactoglobuline lors de la conservation des poudres, en considérant le comportement de sorption d'eau de ces poudres. Les courbes isothermes de sorption d'eau des poudres BL ont été établies. Elles indiquent que toutes les poudres contenant du lactose libèrent de l'eau, mais à des a w différentes selon la teneur en β-lactoglobuline : à a w = 0,43 pour le lactose, à ...

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“…4 Size reduction of protein aggregates (or micronization) with poly(ethylene glycol) (PEG) upon colyophilization 13 can also effectively lead to a more favorable state of the protein, 5,14,15 as seen for nerve growth factor (GF) 16 and albumin, 14 and may also reduce protein adsorption to the polymer matrix. 5,7 Alternatively, the use of saccharides is another approach to protect proteins 4,6,17 by stabilizing proteins through preferential hydration of the native form during lyophilization. 1,6 Sugars were already shown to protect several types of GFs 18 and proteins.…”

mentioning

confidence: 99%

“…5,7 Alternatively, the use of saccharides is another approach to protect proteins 4,6,17 by stabilizing proteins through preferential hydration of the native form during lyophilization. 1,6 Sugars were already shown to protect several types of GFs 18 and proteins. 19 However, while many alternative approaches to GF bioactivity protection have been sought, protein denaturation often remains a key limitation of traditional encapsulation techniques, which has limited the clinical translation.…”

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confidence: 99%