Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters










Database
Language
Publication year range
1.
J Agric Food Chem ; 50(21): 6017-22, 2002 Oct 09.
Article in English | MEDLINE | ID: mdl-12358474

ABSTRACT

Free-standing sterilized edible films based on milk proteins, namely calcium caseinate and whey protein isolate, and polysaccharides, namely pectin and agar, were developed. Cross-linking of the proteins was achieved by the combination of thermal and radiative treatments. Autoclaving pectin and agar prior to their addition to the protein solutions generated films with an improved (P < or = 0.05) puncture strength. The presence of proteins and pectin-agar in the film formulation enhanced (P < or = 0.05) the moisture barrier of the films by 18%. A strain of Streptococcus thermophilus was used to assess the biodegradability behavior of the cross-linked films. Microbiological counts and soluble nitrogen analysis confirmed the biodegradability property of the milk protein films containing autoclaved pectin and agar.


Subject(s)
Agar , Biodegradation, Environmental , Food Microbiology , Food Packaging , Milk Proteins/chemistry , Pectins , Chemical Phenomena , Chemistry, Physical , Colony Count, Microbial , Nitrogen/analysis , Permeability , Streptococcus/isolation & purification
2.
J Agric Food Chem ; 50(21): 6053-7, 2002 Oct 09.
Article in English | MEDLINE | ID: mdl-12358479

ABSTRACT

The contribution of thermal and radiative treatments as well as the presence of some excipients, namely glycerol, carboxymethylcellulose (CMC), pectin, and agar, on the formation of protein-protein interactions as well as the formation and loss of protein-water interactions was investigated by means of differential scanning calorimetry in an isothermal mode. Protein-water interactions were assessed through measurement of the heat of the wetting parameter. Isothermal calorimetry measurements pointed out that gamma-irradiation does not favor protein-water interactions, as reflected by its endothermic contribution (P < or = 0.05) to the heat of wetting values. Although significant (P < or = 0.05), the effect of the thermal treatment on endothermic responses using isothermal calorimetry was found to be somewhat lower. Among excipients added to biofilm formulations, glycerol generated the most important losses of protein-water interactions, as inferred by its significant (P < or = 0.05) endothermic impact on the heat of wetting values.


Subject(s)
Calcium/chemistry , Calorimetry, Differential Scanning/methods , Caseins/chemistry , Cross-Linking Reagents , Food Packaging , Gamma Rays , Hot Temperature , Milk Proteins/chemistry , Agar/pharmacology , Biodegradation, Environmental , Carboxymethylcellulose Sodium/pharmacology , Disulfides/chemistry , Drug Interactions , Food Preservation , Glycerol/pharmacology , Pectins/pharmacology , Thermodynamics , Water , Whey Proteins
3.
J Agric Food Chem ; 49(3): 1397-403, 2001 Mar.
Article in English | MEDLINE | ID: mdl-11312871

ABSTRACT

Sterilized biofilms based on soy protein isolate (SPI, S system) and a 1:1 mixture of SPI and whey protein isolate (WPI, SW system) were achieved through the formation of cross-links by means of gamma-irradiation combined with thermal treatments. The effect of the incorporation of carboxymethylcellulose (CMC) and poly(vinyl alcohol) was also examined. gamma-Irradiation combined with thermal treatment improved significantly the mechanical properties, namely, puncture strength and puncture deformation, for all types of films. Irradiated formulations that contain CMC behave more similarly as elastomers. CMC showed also significant improvements of the barrier properties, namely, water vapor permeability, for irradiated films of the S system and for non-irradiated films of the SW system.


Subject(s)
Milk Proteins/chemistry , Soybean Proteins/chemistry , Carboxymethylcellulose Sodium/chemistry , Gamma Rays , Hot Temperature , Milk Proteins/radiation effects , Polyvinyl Alcohol/chemistry , Soybean Proteins/radiation effects , Whey Proteins
4.
J Agric Food Chem ; 48(12): 6312-6, 2000 Dec.
Article in English | MEDLINE | ID: mdl-11141287

ABSTRACT

Ionizing treatments were applied at 0.5 kGy, 1.5 kGy, and 2.5 kGy to edible mature mushrooms (Agaricus bisporus, albidus) in order to assess the effect of the gamma-irradiation on some biochemical parameters. Irradiation at doses of 1.5 kGy and 2.5 kGy reduced significantly (p < or = 0.05) the rate of respiration of the mushrooms, compared to that of samples irradiated at 0.5 kGy and nonirradiated control samples (C). Ionizing treatments increased significantly (p < or = 0.05) the phenylalanine ammonia-lyase (PAL) activity and total phenols concentration between days 1 and 4. From days 3-4, to the end of the storage period (day 12), both PAL activity and total phenols in the irradiated samples (I) collapsed to lower values. In contrast, the activity of polyphenol oxidase (PPO) increased until days 7, 9, and 12 for samples treated at 0.5, 1, and 2 kGy, respectively. Color measurements showed a loss of whiteness (L value) during storage. After day 4, however, the effectiveness of gamma-irradiation became apparent, and highest L values were obtained for I only.


Subject(s)
Agaricus/metabolism , Phenols/radiation effects , Phenylalanine Ammonia-Lyase/radiation effects , Respiration/radiation effects , Dose-Response Relationship, Radiation , Gamma Rays , Time Factors
5.
J Agric Food Chem ; 46(1): 318-324, 1998 Jan 19.
Article in English | MEDLINE | ID: mdl-10554240

ABSTRACT

gamma-Irradiation was used to produce free-standing sterilized edible films based on caseinate. The effects of calcium ions (Ca(2+)) and two plasticizers, namely propylene glycol (PG) and triethylene glycol (TEG), were investigated, as was the effect of the irradiation on both the gel formation and mechanical properties of the resulting films. gamma-Irradiation provoked formation of bityrosine, i.e., cross-links, accounting for the increase of the puncture strength of films. The presence of PG or TEG enhanced the formation of cross-links, leading to an improved mechanical strength of films. TEG was found to interact more favorably with the caseinate than PG, being responsible for the improved film extensibility. Addition of Ca(2+) caused the formation of gels. The breaking strength of gels was directly related to the concentration of Ca(2+), while the puncture strength of films was found to be almost independent of the calcium concentration. Moreover, a high irradiation dose seemed to affect the protein structure, accounting for the decrease of the breaking strength of gels and for the depreciation of the mechanical behavior of films.

SELECTION OF CITATIONS
SEARCH DETAIL
...