ABSTRACT
Sporeforming bacteria are a significant problem in the food industry as they are ubiquitous in nature and capable of resisting inactivation by heat and chemical treatments designed to inactivate them. Beyond spoilage issues, psychrotolerant sporeformers are becoming increasingly recognized as a potential hazard given the ever-expanding demand for refrigerated processed foods with extended shelf-life. In these products, the sporeforming pathogens of concern are Bacillus cereus, Bacillus weihenstephanensis, and Clostridium botulinum type E. This review article examines the foods, conditions, and organisms responsible for the food safety issue caused by the germination and outgrowth of psychrotolerant sporeforming pathogens in minimally processed refrigerated foods.
Subject(s)
Bacillus/growth & development , Botulism/microbiology , Clostridium botulinum/growth & development , Food Safety , Food Storage/standards , Foodborne Diseases/microbiology , Bacillus cereus/growth & development , Botulism/prevention & control , Cold Temperature , Food Microbiology , Food Preservation , Food Storage/methods , Foodborne Diseases/prevention & control , Spores, BacterialABSTRACT
High-pressure processing (HPP) was utilized to induce unfolding of beta-lactoglobulin (beta-LG). beta-Lactoglobulin solutions at concentrations of 0.5 mg/mL, in pH 7.5 phosphate buffer, were pressure treated at 510 MPa for 10 min at either 8 or 24 degrees C. The secondary structure, as determined by circular dichroism (CD), of beta-LG processed at 8 degrees C appeared to be unchanged, whereas beta-LG processed at 24 degrees C lost alpha-helix structure. Tertiary structures for beta-LG, as determined by near-UV CD, intrinsic protein fluorescence spectroscopy, hydrophobic fluorescent probe binding, and thiol group reactivity, were changed following processing at either temperature. The largest changes to tertiary structure were observed for the samples processed at 24 degrees C. Model solutions containing the pressure-treated beta-LG showed significant decreases in surface tension at liquid-air interfaces with values of 54.00 and 51.69 mN/m for the samples treated at 24 and 8 degrees C, respectively. In comparison, the surface tension for model solutions containing the untreated control was 60.60 mN/m. Changes in protein structure during frozen and freeze-dried storage were also monitored, and some renaturation was observed for both storage conditions. Significantly, the sample pressure-treated at 8 degrees C continued to display the lowest surface tension.
Subject(s)
Cold Temperature , Lactoglobulins/chemistry , Chemical Phenomena , Chemistry, Physical , Circular Dichroism , Freezing , Hot Temperature , Hydrogen-Ion Concentration , Molecular Structure , Pressure , Protein Folding , Solutions , Spectrometry, Fluorescence , Structure-Activity RelationshipABSTRACT
Ultra-high pressure (200, 270 and 340 MPa), temperature (~4, 21 and 38°C), and time (5, 15, 40 and 60 min) combinations were evaluated as a means to extend the shelf-life of fresh cut pineapple chunks. Cut pineapple obtained from an industrial processor was packed in heat-sealed polyethylene pouches. Triplicate samples were temperature adjusted and treated in an Autoclave Engineers IP2-22-60 isostatic press. Surviving bacteria and total yeast and mold counts were determined using plate count agar (PCA) and acidified potato dextrose agar (PDA), respectively. At the highest pressure (340 MPa) and 15 min, decimal reductions measured by growth on PCA were 3.0 (~4°C), 3.1 (21°C) and >2.5 (38°C). Pressure treated pineapple pieces had PCA counts < 50 colony forming units (CFU)/g. At 270 MPa and 15 min, greater than two decimal reductions were observed only at 38°C. Exposure to pressures of 200 MPa resulted in about one decimal reduction in PCA counts for all temperature and time combinations tested. PDA counts followed a similar behavior for all pressure treatments.
