HOMEBREW Digest #5005 Thu 11 May 2006

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  Wondering about what CEP requires... ("Bev D. Blackwood II")
  Re: Rust on diffusion stone ("Alex Sheftel")
  Re: rust on diffusion stone (Randy Ricchi)
  Cross Postings among various lists ("Terry Felton")
  Roggenbier and enteropathy Part 1 of 2 ("Dave Burley")
  Roggenbier and enteropathy now part 2 of 3 parts ("Dave Burley")
  Roggenbier and enteropathy now part 3 of 3 ("Dave Burley")
  All quiet on the HBD (RiedelD)
  Reviving/using possibly autolyzed yeast (RiedelD)

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---------------------------------------------------------------------- Date: Wed, 10 May 2006 22:45:28 -0500 From: "Bev D. Blackwood II" <bdb2 at bdb2.com> Subject: Wondering about what CEP requires... Are there exams at the end of the NHC sessions that will earn CEP points? I don't know what to expect.... -BDB2 Bev D. Blackwood II http://www.bdb2.com Return to table of contents
Date: Thu, 11 May 2006 08:00:13 -0400 From: "Alex Sheftel" <asheft at po-box.mcgill.ca> Subject: Re: Rust on diffusion stone Jim, As far as your health and that of your guests, a little rust in your beer will not be dangerous. In the low pH of wort, it is possible that the rust will dissolve, but with the added oxygen, it is also possible that the dissolved iron will precipitate as ferric hydroxide and be gone with your trub. Either way, it will not be dangerous to consume a little rust. (For what it's worth, I am at the tail end of a PhD on mammalian iron metabolism.) Having said that, I do not recommend that anyone eat large quantities of rust. I also cannot comment on how the small amount of metal might affect the flavour of your beer (since you can't specify the amount of rust and didn't mention the volume of your batch and I don't know the taste threshold for iron). Happy Brewing, Alex Return to table of contents
Date: Thu, 11 May 2006 08:26:42 -0400 From: Randy Ricchi <rricchi at houghton.k12.mi.us> Subject: Re: rust on diffusion stone Jim, I doubt that that little spot of rust is going to do any harm to your beer, given the short contact time and all. But, if you have time, here's a way to get rid of it: I had the same thing with my stone, and I filled a little cup with CLR (Calcium, Lime, Rust) remover, dropped the stone in and left it overnight. The next morning I rinsed the heck out of it and ran water through it. Worked like a charm, AND, I believe it actually cleaned unseen deposits out of the pores in the stone, because before the cleaning, when I'd run water into the stone, it wouldn't seep through on it's own but had to be blown through. After the cleaning the water would seep through on it's own. It's been years since I did this and I'm still using the same stone, and haven't had a recurrence of rust. I think CLR comes in a green pint or quart size plastic bottle; you can probably find it at Wal-Mart or hardware stores, it's a pretty common product. Return to table of contents
Date: Thu, 11 May 2006 11:10:54 -0400 From: "Terry Felton" <tdfelton at gmail.com> Subject: Cross Postings among various lists I normally would not send the same post to three lists at once, but in this case it seems necessary. I must echo the concerns raised recently on the Judgenet by Steve Stroud, about inappropriate issues being posted all over the place. I try to follow 3 lists, "AHA Tech Talk", the "HBD Forum", and the "JudgeNet" of the BJCP. In the past, each had it's clear focus, and there was little duplication among them, other than some occasional competition notices. In the last few weeks, it is becoming increasingly difficult to differentiate among them, since several people are posting the same stuff on two or three, almost indiscriminately. Please everybody, can we stop shouting all over the place? Leave the Judgenet for BJCP and judging related matters, address AHA issues, (along with general technical brewing questions) in the AHA Tech Talk, and cover remaining stuff in the more broadly rooted HBD Forum. I don't mean to say that there should never be duplication, or off topic stumbles, but the character of all these venues has decidedly changed for the worse in recent weeks. I hope the members and participants at all three can return us to the high standards we used to expect from all three of these fine forums. Now, let's all relax and have a homebrew, Terry Felton AHA member and BJCP Judge Return to table of contents
Date: Thu, 11 May 2006 11:47:02 -0400 From: "Dave Burley" <Dave_Burley at charter.net> Subject: Roggenbier and enteropathy Part 1 of 2 Brewsters: Been too busy to comment,but I read every isssue of HBD. Peter Ensminger commments that Rye grain has lots of gluten. Peter says: "Roggen (German for "Rye") is especially high in gluten. How can you make a gluten-free Roggenbier?" This does not match to my understanding of "especially high", but for sure rye does contain gluten. Peter, as you know I do a lot of sourdough bread baking ( as well as produce roggenbier using a fast sparge followed by a slow one hot one to avoid sparging problems). My recollection is that it is not the gluten in <true> 100% rye bread ( no wheat or wheat gluten) that forms a somewhat risen, heavy loaf but other gum components of the rye which trap a msmallpercentage of the CO2 generated by the microbes. It is these gum components which can cause stuck sparges. High temperature sparges are a must, and why I remove the wort quickly, heat it up, pour it backover the grains and re-sparge it slowly with higher temperature sparge water. True rye bread is prepared with an acid starter and allowed to stand a day or two after baking and before being cut to avoid stickiness, which the acid helps reduce. Here are some additional comments on the subject which show just how sensitive some immune systems can be to even minute wheat cross contamination. This makes me wonder if the reaction to rye is not due in some part to the processng of wheat and rye flours in the same facility. With a limited search I cannot find an actual comparison of gluten content in these grains of interest to us brewers. More refined studies (as I recall) indicate it is the gliadin and not glutelin ( the two proteins in "gluten" and both needed in wheat bread rising) that is the protein causing the reaction to "gluten" and why food researchers are reexamining this question. Here are some selected references: http://www.gicare.com/pated/edtgs06.htm Gluten is the protein part of wheat, rye, barley, and other related grains. Some people cannot tolerate gluten when it comes in contact with the small intestine. This condition is known as celiac disease (sometimes called non-tropical sprue or gluten sensitive enteropathy). There is also evidence that a skin disorder called dermatitis herpetiformis is associated with gluten intolerance. ..... Oats is a grain the merits special attention. Oats are believed safe in patients with celiac disease although this was not always the case. The problem with oat products is not the grain but rather the manufacturing process. When oats are processed in the same facilities as wheat, contamination can occur even with the best cleaning protocol. Oat products can now be found that are not cross contaminated. These can be tried after an initial period of 6 months to see if they can be tolerated. Most, but not all patients can tolerate pure oat products. - -------------- http://www.frysfood.com/hn/Food_Guide/Rye.htm Celiac disease (also called gluten-induced enteropathy) is an intestinal disorder caused by intolerance to gluten, a protein found in wheat, barley, and rye. While oats contain a substance similar to gluten, modern research has found that eating moderate amounts of oats does not appear to cause problems for people with celiac disease. - --------------------- http://www.grindstonebakery.com/rye.htm Rye is a member of a non-scientifically established grain group traditionally called the "gluten grains." The idea of grouping certain grains together under the label "gluten grains" has come into question in recent years as technology has given food scientists a way to look closer at the composition of grains. Some healthcare practitioners continue to group wheat, oats, barley and rye together under the heading of "gluten grains" and to ask for elimination of the entire group on a wheat-free diet. Other practitioners now treat wheat separately from these other grains, including rye, based on recent research. Wheat is unquestionably a more common source of food reactions than any of the other "gluten grains," including rye. See Part 2 for some hope - -------------------------- Keep on Brewin' Dave Burley Return to table of contents
Date: Thu, 11 May 2006 12:14:49 -0400 From: "Dave Burley" <Dave_Burley at charter.net> Subject: Roggenbier and enteropathy now part 2 of 3 parts Brewsters: Part 2 of 3 There is some hope for brewing beer from gluten containing grains. The use of aspegrgillus niger amylase enzymes can break down protein/carbohydrates and the <<<<carbohydrates>>>> which seem to be the agent that stirs up the production of T cells and causes the breakdown of the villi in the intestine of celiacs. We know that malting and brewing times and temperatures can affect the content of small protein/peptides/carbohydrates and therefore suggests a pathway to reduce these in the beer. This obviously needs a lot of experimentation, but the direction is tempting. Here is extracted information. Full articles are in the references. - --------------------- http://www.enzymestuff.com/conditionceliac.htm Celiac and Enzymes last updated 5.7.06 Totally awesome site for information on celiac, see www.celiac.com Research on enzymes for celiac Celiac is a very serious condition, which often goes undiagnosed. So if someone sees regression with gluten + enzymes, particularly strong proteases such as Peptizyde, they are advised to consider celiac as a possibility. .... There are three common theories being discussed as the cause for celiac and the specific amino acid sequences have not been identified. It is an autoimmune reaction with a genetic basis. There is a certain structure in the gliadin that the small intestine sees as toxic in celiac individuals. The protease enzymes are not breaking this down in a way so that it does not cause a reaction in celiacs. ( See paper below-DRB) So, in fact, taking just a protease such as Peptizyde may be just making more of these little peptides (or whatever) available to the small intestine, and perhaps increasing the number of chances to provoke a reaction. There was some research on the www.celiac.com site which proposed this same thing with the use of barley enzymes although it also said this was just a working theory and there was no evidence to back it up. No two celiacs are alike in their dietary tolerances for gluten - some are very sensitive, some can tolerate a little at a time, some can't take oats or spelt or kamut, some can. So if a person suspects celiac, takes Peptizyde and gluten and doesn't do well, that person should avoid gluten under all circumstances. ....... - --------- Amylase/Glucoamylase May Help Celiacs with Gluten After the above was written, the following article below was found and describes the situation with references. <<Apparently the part of the gliadin in gluten that causes problems to a person with celiac is not the protein or peptides derived from the protein, it is portions of gliadin carbohydrate.>> Although the protein can antagonize the situation (and cause the peptide probelm), <<<the enzymes needed to break down the part of gliadin reactive to celiacs are the amylases (known to exist in malt - DRB) and some subgroups of amylases (other enzymes that work on starch bonds such as glucoamylases).>>> This correlates exactly to what we have seen with many families using enzymes. The proteases create more, smaller pieces but would not necessarily break down the carbohydrate bonds (if at all), thus making the situation for a celiac eating gluten with protease enzymes worse than if they ate gluten without protease enzymes. It also follows that some people with suspected celiac have done better with the the amylase containing enzymes with gluten. <<<So a person with suspected celiac should be taking enzymes for carbs with gluten contamination or infractions as well, not just the proteases.>>> ....... Both amylase and glucoamylase need to be in a product. If you think of starches as a tree, the amylase will work on from the end of branch inward, til it comes to a fork, where it stops because the glycosidic linkage is different. Glucoamylase, however, cleaves the fork, which then allows amylase to continue. That is why amylase should always be accompanied by glucoamylase, otherwise, the starch cleavage is not very effective. Same with the other carbohydrases. They work on one type of glycosidic linkage, and a carb may have many kinds of linkages present. The carbohydrate on gliadin is very complex, consisting of xylose, glucose, galactose, and arabinose. It is typical of plant cell walls which contain hemicellulase, pectin, lignin, and other sugars. One needs a complex of carbohydases to extensively degrade them. See hope for brewers in part 3 Keep on Brewin' Dave Burley Return to table of contents
Date: Thu, 11 May 2006 12:17:15 -0400 From: "Dave Burley" <Dave_Burley at charter.net> Subject: Roggenbier and enteropathy now part 3 of 3 Brewsters: The article continues from part 2: "I checked several of the references at Pubmed and the articles are listed there. On pages 598-599 of the Pharmacology of Natural Medicines, there is this information: "It has been known since the 1950s that the gluten found in wheat, rye and other grains is the cause of intestinal damage in celiac disease, with the gliadin fraction of gluten being the source of its toxicity. [references 1,2] By the 1970s, fractionation studies had succeeded at identifying the components of gliadin involved in teh toxic mechanism. The carbohydrate moiety, consisting mainly of glucose, galactose, xylose and arabinose, is the source of gluten's gastrointestinal toxicity in the celiac patient, rather than the protein fraction as had been previously suspected. [3,4,5] "Amylytic enzymes from Aspergillus species are effective in vitro in the treatment of celiac disease, as they enzymatically cleave the toxic carbohydrate portion of gliadin. Fungal carbohydrase preparations render grains like wheat and rye virtually harmless to individuals with gluten enterophathy. A 1977 study attempting to identify the source of gliadin toxicity used a preparation of amylytic enzymes from Aspergillus niger to remove the carbohydrate portion of gliadin in vitro. To be certain of the variables being tested, native gliadin was chromatographed showing that carbohydrate was associated with four main protein bands. When the carbohydrase-treated gliadin was chromatographed, no alteration was detected in the protein pattern, but carbohydrate was completely absent. To further establish that the protein make-up remained unchanged as compared with native gliadin, peptide mapping of the treated gliadin was carried out using electrophoresis followed by chromatography. Peptide maps showed no difference between the treated and untreated gliadin, confirming that no alteration had occurred in the primary structure of the protein. Gliadin treated in this manner was baked into loaves of bread made with gluten-free flour. The study compared the effect of bread with treated versus untreated gliadin on four patients with previously diagnosed celiac disease. All four patients had been on gluten-free diets for at least 3 months prior to the study and were virtually symptom-free. Previously, their clinical and physical signs and symptoms had included the diarrhea, malabsorption, decreased body weight and height, anemia, tetany, impaired D-xylose absorption, decreased intestinal mucosal enzyme secretion flattened mucosal brush-border and subepithelial tissue lymphocytosis typical of celiac disease. During the test period, patients 1,2, and 3 received a total of 50g of treated gliadin baked into loaves of bread (10g gliadin/450 g loaf). Xylose absorption tests and intestinal biopsies from jejunal villi were performed before and after each test period. The celiac patient receiving untreated gliadin (patient no 4) experienced a return of signs and symptoms of celiac disease - diarrhea, abdominal pain, low values on xylose absorption studies, decreased mucosal enzyme secretion (alkaline phosphates, lactase, surcease) and characteristic histological damage (mucosal lumphocytosis and loss of enterocyte height). The patients who received the treated glidin remained symptom-free during the test period and showed no abnormalitites in histological parameters (i.e. general morphology, epithelial cell height, tissue lymphocytes were normal in these patients). And the good news - DRB - is: <<<This study demonstrated that carbohydrate-digesting enzymes from Aspergillus sp. can be used in vitro to remove the toxicity of gluten to celiac patients and supports the hyypothsis that carbohydrate components of gliadin are responsible for its toxicity, rather than protein components as had been widely suspected.>>> It appears that no controlled studies have been done to evaluate the effectiveness of amylytic fungal enzymes at reducing gluten toxicity to celiac patients in vivo by administering these enzymes with gluten containing foods at mealtime. <<<It should be noted that although celiac patients show intolerance to the carbohydrate portion of gliadin, this is likely not he only source of gluten-induced pathology.>>> A number of studies suggest that protein components of gluten produce systemic allergic manifestations in some patients. It appears that both gastrointestinal intolerance and immunological hypersensititity are capable, either individually or in concert, of producing disease symptoms in susceptible individuals. Future studies may also show that both pathological mechanisms are amenable to treatment by hydrolysis of the offending portions of gluten with the appropriate orally administered fungal enzymes. This, however, remains to be proven." 1.Dicke WK. An investigation into the injurious constituents of wheat in connection with their action on patients with Coeliac disease. Acta Pediatr 1953; 42:223-231 2.Van De Kamer JH, Weijers HA, Coeliac disease: some experiments on the cause of the harmful effect of the gliadin. Acta Pediatr 1955; 44: 465-469 3.Phelan JJ, Stevens FM, McNicholl B et a. Coelic disease: the abolition of gliadin toxicity by enzymes from Asergillus niger. Clin Sci Molec Med 1977; 53: 35-43 4.McCarthy CF. Nutritional defects in patients with malabsorption. Proc Nutr Soc 1976; 35:37-40 5.Phelan JJ. The nature of gliadin toxicity in celiac disease. Biochem Soc Trans 1974; 2:1368-1370 6.Hekkens WTMJ et al. Antibodies to gliadin in serum of normals, celiac patients and schizophrenics. Nature 1963; 199; 259-261" Research on Enzymes for Celiac Stanford researchers find cause, possible cure for gluten intolerance >From http://www.eurekalert.org/pubnews.php?start=25 Public Release: 26-Sep-2002 Stanford researchers find cause, possible cure for gluten intolerance A team of investigators led by Stanford University researchers have discovered the cause and a potential treatment for celiac sprue, an autoimmune disease that leads to an inability to digest gluten, a major protein in wheat, rye and barley products. - National Science Foundation (Here's the article. Note the last line - "We think that this mode of therapy - peptidase supplementation - may offer hope in treating celiac sprue eventually, and we're going to test this hypothesis.") >From http://www.eurekalert.org/pub_releases/2002-09/sumc-srf092402.php Stanford researchers find cause, possible cure for gluten intolerance Public release date: 26-Sep-2002 ........ Because the fragment is rich in the amino acid proline, investigators reasoned that a peptidase (an enzyme that breaks down proteins) with the ability to digest proline-rich chains might be able to break down the gliadin fragment, rendering it harmless to celiac patients. They have now shown that this is the case in test tubes and in rats. Because there are no animal models of celiac disease, testing this approach in humans is a long way off and will require further preclinical work, <<<<Khosla said. "We think that this mode of therapy - peptidase supplementation - may offer hope in treating celiac sprue eventually, and we're going to test this hypothesis.">>>> - ---------------------------------- Let's hope. Some research results may now be available. Keep on Brewin' Dave Burley Return to table of contents
Date: Thu, 11 May 2006 11:14:20 -0700 From: RiedelD at pac.dfo-mpo.gc.ca Subject: All quiet on the HBD So, it seems our beloved HBD is getting less use these days. Those of us who have been reading the digest for years probably have less things to post on than we used to, but assuming that there are always new brewers around with questions and experiences to share, I'm wondering where all the discussion has gone? Where is all the good brewing talk on the 'net these days? Dave Riedel Victoria, BC, Canada Return to table of contents
Date: Thu, 11 May 2006 11:22:26 -0700 From: RiedelD at pac.dfo-mpo.gc.ca Subject: Reviving/using possibly autolyzed yeast I can't really complain that the HBD is slowing down without contributing something, so here goes: Recent discussions about storing yeast under beer ended with comments to the effect that even if autolysis had occurred, you could still use the yeast. I'm assuming that the best way to do this would be to pitch into a starter, aerate, and harvest the yeast off the top to ensure that the healthier cells would be selected and the autolysed yeast and nasty beer would be left behind. Fair enough? Dave Riedel Victoria, Canada Return to table of contents
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