Human pancreatic juice was used as a source of amylase, lipase, trypsin, and chymotrypsin. The human pancreatic juice was incubated with one of several dietary fibers, including alfalfa, oat bran, pectin. Solka Floc, wheat bran, and xylan. In addition, the human pancreatic juice was incubated without any fiber, which was used as the control. Incubation with Solka Floc (cellulose) and xylan (a hemicellulose) resulted in a substantial loss of activity in all enzymes assayed. Wheat bran and oat bran decreased amylase and chymotrypsin activity, while alfalfa decreased trypsin and chymotrypsin activity. Incubation with pectin significantly increased amylase and chymotrypsin activity. The mechanism by which sources of dietary fiber can alter enzyme activity is currently unknown. This effect of a dietary component on the activity of human pancreatic enzymes emphasizes the need to investigate further the effects of dietary fiber on digestion and absorption in the small intestine to understand fully its effects on metabolism.
Food allergies affect an estimated 10 to 12 million people in the United States. Some of these individuals can develop life-threatening allergic reactions when exposed to allergenic proteins. At present, the only successful method to manage food allergies is to avoid foods containing allergens. Consumers with food allergies rely on food labels to disclose the presence of allergenic ingredients. However, undeclared allergens can be inadvertently introduced into a food via cross-contact during manufacturing. Although allergen removal through cleaning of shared equipment or processing lines has been identified as one of the critical points for effective allergen control, there is little published information on the effectiveness of cleaning procedures for removing allergenic materials from processing equipment. There also is no consensus on how to validate or verify the efficacy of cleaning procedures. The objectives of this review were (i) to study the incidence and cause of allergen cross-contact, (ii) to assess the science upon which the cleaning of food contact surfaces is based, (iii) to identify best practices for cleaning allergenic foods from food contact surfaces in wet and dry manufacturing environments, and (iv) to present best practices for validating and verifying the efficacy of allergen cleaning protocols.
The control of food allergens in a food-processing plant presents numerous challenges. An allergen prevention plan must determine potential sources of contaminating allergens and appropriate controls to prevent their introduction into food products. These controls may include scheduling production of allergen-containing products at the end of manufacturing runs, appropriate labeling and use of rework, equipment and system-design considerations, and thorough cleaning of lines after running allergen-containing food products. Proper labeling of food products, effective management of label inventories, control of ingredients from suppliers, and training of employees are key factors in allergen control.
Previous studies have shown that the development in rats of aflatoxin B1 (AFB1)-induced gamma-glutamyl transpeptidase-positive (GGT+) foci, indicators of early preneoplastic liver lesions, was markedly greater when a 20% casein diet was fed than when a 5% casein diet was fed during the postinitiation period. In the present study, the dose-response relationship between dietary protein level (dose) and emergence of AFB1-induced GGT+ foci (response) in livers of rats was determined. Male Fischer-344 rats fed a 20% casein diet were orally administered AFB1 at a dose level of 250 micrograms/(kg X d) (10 doses over 12 d). One week after the last dose, the animals were divided into eight groups and fed isoenergetic diets containing either 4, 6, 8, 10, 12, 15, 20 or 30% dietary casein for the remaining 12 wk of the study. The development of GGT+ foci, as measured by number and percent of liver volume occupied, displayed a response with three discrete phases. The lowest dietary protein levels, 4, 6, 8 and 10% casein, were associated with a minimal level of GGT+ foci development. Between 10 and 12% dietary casein, the development of GGT+ foci sharply increased, up to the 15-30% dietary casein level. The sudden increase in the formation of GGT+ foci at 10-12% dietary casein was just above the level of dietary casein (6-8%) required for maximum body weight gain. These results in this animal model suggest that protein intake in excess of that required to sustain maximum growth rate may enhance AFB1-induced cancer development.
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