Isinglass

Abstract: Objective: Recent Australian and international legislation requires labeling of wines made by using the potentially allergenic food proteins casein, milk, egg white, or isinglass (fish-derived) where "there is a detectable residual processing aid." We investigated whether wines fined using these proteins or non-grape-derived tannins (tree-nut derived) can provoke significant clinical allergic reactions (anaphy- laxis) in patients with confirmed immunoglobulin E-mediated relevant food allergy. Methods: A double-blind, placebo-controlled trial was performed to determine whether allergic reactions followed consumption of Australian commercial wines fined using one or more of the legislation-targeted food proteins. In addition, allergenicity of a larger panel of these wines was evaluated by blood basophil activation. Results: No anaphylaxis was induced by wine consumption. Three mild clinical reactions to protein-fined wine and two mild reactions to unfined wine occurred, but there was no statistically significant difference in reaction parameters between subject groups or between processing aids. No pattern of basophil activation correlated with wine type, processing aid, or subject group. Conclusion: Wines fined with egg white, isinglass, or non-grape-derived tannins present an extremely low risk of anaphylaxis to fish-, egg-, or peanut-allergic consumers. Although consumption of milk protein-fined wine did not induce anaphylaxis, there were insufficient subjects to determine statistically whether wines fined with milk proteins present a risk to the very rare milk-allergic consumers. In summary, the observed lack of anaphylaxis and basophil activation induced by wines made using the legislation-targeted food proteins according to good manufacturing practice suggests negligible residual food allergens in these wines. © 2006 Elsevier Inc. All rights reserved.

Abstract: The effect of several proteins on three main wine proanthocyanidin containing fractions with the mean degree of polymerization (mDP) of 1.5 (FI), 3.4 (FII), and 4.9 (FIII) was studied. Although casein and potassium caseinate showed similar molecular weight (MW) distribution, casein decreased the FI fraction more than the twice as effectively as potassium caseinate. A gelatin with a medium MW polydispersion induced a similar decrease (~20%) in all tannin fractions. A gelatin with low MW primarily removed the tannin fractions of lower mDP (FI and FII), while a gelatin with a higher MW had a minor effect (5%) on the fraction of higher mDP (FIII). Neither of the two studied isinglasses reduced the FII fraction. The tannins of FI and FIII were removed by swim bladder isinglass twice as effectively as by fish skin isinglass. For the mDP of fined wines, egg albumin induced a decrease on mDP of 24% for the more polymerized tannin fraction (FIII); although within all assays there was a decrease ranging from 6 to 14%.

Abstract: Food allergy can cause food-related anaphylaxis. Food allergen labeling is the principal means of protecting sensitized individuals. This motivated European Directive 2003/89 on the labeling of ingredients or additives that could trigger adverse reactions, which has been in effect since 2005. During this study, we developed animal models with allergy to ovalbumin, caseinate, and isinglass in order to be able to detect fining agent residues that could induce anaphylactic reactions in sensitized mice. The second aim of the study was to design sandwich ELISA tests specific to each fining agent in order to detect their residue antigenicity, both during wine processing and in commercially available bottled wines. Sensitized mice and sandwich ELISA methods were established to test a vast panel of wines. The results showed that although they were positive to our highly sensitive sandwich-ELISA tests, some commercially available wines are not allergenic in sensitized mice. Commercially available bottled wines made using standardized processes, fining, maturation, and filtration, do not therefore represent any risk of anaphylactic reactions in sensitized mice.