Increasing consumer demand for safer foods and longer product shelf life is forcing the industry to develop new food-processing, and packaging strategies. The food industry uses a wide range of non-edible packaging materials and various biodegradable protein- and polysaccharide-based films that might act not only as packaging materials, but also as carriers for a number of food additives. including antimicrobial proteins, that have already been incorporated into edible films in order to retard surface growth of bacteria, yeasts, and molds on a wide range of products, since they offer the advantage of being safe for the consumer: specific in their action (in particular towards food-borne pathogens); and active at low concentrations. In our study, we addressed the issue of possible structural and functional changes ensuing from the interaction of various antimicrobial proteins either with cellulose-based packaging materials (paper and paper derivatives), or with polymers that may be incorporated into, or layered onto, a suitable packaging material. Binding of the antimicrobial proteins to various matrices was studied by a number of approaches, including dynamic light scattering in the case of soluble polymers. The stability of the interaction was assessed under a variety of conditions (pH, ionic strength, presence of other food components) that may result in a stripping of the protein. Structural changes ensuing from binding of antimicrobial proteins to a variety of matrices were studied spectroscopically either in solution or by using solid-state techniques. such as front-face spectrofluorimetry [1], and thin-film circular-dichroism. Our results show that immobilization on appropriate substrates affects only marginally the structural and functional properties of antimicrobial proteins. The same approaches were also used to study changes in the thermal sensitivity of the structural features of the immobilized proteins, given their relevance to the processing of pre-packaged foods. Our studies show that immobilization facilitates the recovery of structural features in the antimicrobial proteins alter heat treatment. References 1 Bonomi F et al Anal. Biochem. 2004, 329: 104-111
Biotechnology for Food Protection: Structural Features of Immobilized Antimicrobial Proteins
Marengo M;
2007-01-01
Abstract
Increasing consumer demand for safer foods and longer product shelf life is forcing the industry to develop new food-processing, and packaging strategies. The food industry uses a wide range of non-edible packaging materials and various biodegradable protein- and polysaccharide-based films that might act not only as packaging materials, but also as carriers for a number of food additives. including antimicrobial proteins, that have already been incorporated into edible films in order to retard surface growth of bacteria, yeasts, and molds on a wide range of products, since they offer the advantage of being safe for the consumer: specific in their action (in particular towards food-borne pathogens); and active at low concentrations. In our study, we addressed the issue of possible structural and functional changes ensuing from the interaction of various antimicrobial proteins either with cellulose-based packaging materials (paper and paper derivatives), or with polymers that may be incorporated into, or layered onto, a suitable packaging material. Binding of the antimicrobial proteins to various matrices was studied by a number of approaches, including dynamic light scattering in the case of soluble polymers. The stability of the interaction was assessed under a variety of conditions (pH, ionic strength, presence of other food components) that may result in a stripping of the protein. Structural changes ensuing from binding of antimicrobial proteins to a variety of matrices were studied spectroscopically either in solution or by using solid-state techniques. such as front-face spectrofluorimetry [1], and thin-film circular-dichroism. Our results show that immobilization on appropriate substrates affects only marginally the structural and functional properties of antimicrobial proteins. The same approaches were also used to study changes in the thermal sensitivity of the structural features of the immobilized proteins, given their relevance to the processing of pre-packaged foods. Our studies show that immobilization facilitates the recovery of structural features in the antimicrobial proteins alter heat treatment. References 1 Bonomi F et al Anal. Biochem. 2004, 329: 104-111
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