Effect of polysaccharides on the stability and renaturation of soybean trypsin (Kunitz) inhibitor

Burova, Tatiana V.; Varfolomeeva, E. P.; Grinberg, V. Ya.; Haertlé, Thomas; Tolstoguzov, V. B.

doi:10.1002/1616-5195(200208)2:6<286::aid-mabi286>3.0.co;2-b

Cited by 24 publications

(15 citation statements)

References 23 publications

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“…It was suggested that similar destabilisation may occur for other proteins upon interaction with highly charged polymeric compounds or surfaces. However, some studies also show that complexation of the protein with a polysaccharide can preserve the functionality of the protein and prevent denaturation (Burova, Varfolomeeva, Grinberg, Haertle´, & Tolstoguzov, 2002;Ivinova, Izumdurov, Munoretz, Galaev, & Mattiasson, 2003).…”

Section: Introductionmentioning

confidence: 43%

The effect of heating on β-lactoglobulin–chitosan mixtures as influenced by pH and ionic strength

et al. 2008

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Section: Introductionmentioning

confidence: 43%

The effect of heating on β-lactoglobulin–chitosan mixtures as influenced by pH and ionic strength

et al. 2008

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“…Similar effects were observed for other protein-poly electrolyte systems [22][23][24][25][26]. The probable cause of enzyme destabilization is that the unfolded protein is preferably bound by the polymer matrix [23,45]. However, it is important that soybean peroxidase in the bound state retains its tertiary structure.…”

Section: Conformational Stability Of Soybean Peroxidase and The Nipa-supporting

confidence: 40%

“…These centers may be neg atively or positively charged groups, specifically, car boxyl, sulfonate, or trimethylammonium. Despite a considerable bulk of studies dealing with the inter polyelectrolyte complexes of proteins [22][23][24][25][26], the systematic data on conformational changes in ther moresponsive polymers and globular proteins result ing from complexation are very scanty. There are almost only single facts derived by indirect methods [27][28][29][30].…”

Section: Introductionmentioning

confidence: 45%

Interpolyelectrolyte complexes of soybean peroxidase with thermoresponsive copolymers

et al. 2012

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Interpolyelectrolyte complexes of soybean peroxidase with thermoresponsive N isopropylacryla mide-sodium styrenesulfonate copolymers of various compositions are studied by the methods of high sen sitivity differential scanning calorimetry, velocity sedimentation, and nephelometry. It is shown that the enzyme preserves its tertiary structure in complexes, although the conformational stability of bound protein is lower than that of free protein. Complexes of any compositions, including stoichiometric complexes, are soluble at room temperature but precipitate during heating in the region of the conformational transition of the copolymer accompanied by formation of the complex gel. Isotherms of enzyme binding by complex gels are constructed, and their analysis makes it possible to reveal two types of binding in the system: a relatively strong stoichiometric binding of the enzyme with the copolymers and a weaker binding of the protein in the coacervate phase of the complex gel. A high yield of the protein in the complex gel, reversibility of binding, and preservation of the tertiary structure of the enzyme in complexes with the copolymers make proteinthermoresponsive polyelectrolyte systems promising for bioseparation.

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“…Protein renaturation in material matrices has been previously reported. For example, soybean protease inhibitors can renature after thermal denaturation by binding to polysaccharides [42]. Altamirano et al [43] attached the enzymes (glucosamine 6-phosphate deaminase, indole 3-glycerol phosphate synthase, cyclophilin A, firefly luciferase) to agarose gels and found this strategy could be used for efficient renaturation of the proteins.…”

Section: Discussionmentioning

confidence: 99%

Stabilization of Enzymes in Silk Films

et al. 2009

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Material systems are needed that promote stabilization of entrained molecules, such as enzymes or therapeutic proteins, without destroying their activity. We demonstrate that the unique structure of silk fibroin protein, when assembled into the solid state, establishes an environment that is conducive to the stabilization of entrained proteins. Enzymes (glucose oxidase, lipase and horseradish peroxidase) entrapped in these films over ten months retained significant activity, even when stored at 37°C, and in the case of glucose oxidase did not lose any activity. Further, the mode of processing of the silk protein into the films could be correlated to the stability of the enzymes. The relationship between processing and stability offers a large suite of conditions within which to optimize such stabilization processes. Overall, the techniques reported here result in materials that stabilize enzymes to a remarkable extent, without the need for cryoprotectants, emulsifiers, covalent immobilization or other treatments. Further, these systems are amenable to optical characterization, environmental distribution without refrigeration, are ingestible, and offer potential use in vivo, since silk materials are biocompatible and FDA approved, degradable with proteases and currently used in biomedical devices.

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Effect of polysaccharides on the stability and renaturation of soybean trypsin (Kunitz) inhibitor

Cited by 24 publications

References 23 publications

The effect of heating on β-lactoglobulin–chitosan mixtures as influenced by pH and ionic strength

The effect of heating on β-lactoglobulin–chitosan mixtures as influenced by pH and ionic strength

Interpolyelectrolyte complexes of soybean peroxidase with thermoresponsive copolymers

Stabilization of Enzymes in Silk Films

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