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Celiac.com 10/10/2017 - If you're looking for a delicious, easy to make meal that is perfect for the start of fall, this slow-cook chicken vegetable soup is just the thing. Ingredients: 2 chicken thighs, skin removed 1½ cups zucchini, halved lengthwise and sliced 1 cup yellow onion, chopped 1 cup celery, chopped 4 large cloves garlic, chopped 3 thyme sprigs, fresh 1 tablespoon chopped fresh sage 2 tablespoons vegetable oil 8 cups unsalted chicken broth 3 large carrots, diagonally sliced (2 cups) 2 large parsnips, peeled and chopped 3 cups chard, chopped ½ cup uncooked wild rice 2 teaspoons kosher salt 1 teaspoons black pepper 2 tablespoons fresh lemon juice Directions: Combine onion, celery, garlic, thyme, sage, and 1 tablespoon oil in a large slow cooker. Cover and cook on high until vegetables have slightly softened, about 10-12 minutes. Meanwhile, heat remaining 1 tablespoon oil in a large skillet over medium-high heat. Add chicken thighs; cook until well browned on all sides, about 3 minutes per side. Transfer to slow cooker; add broth, carrots, and parsnips. Reduce heat to low, cover, and cook until turkey is very tender, about 4 hours. Remove chicken thighs from slow cooker. Cut meat from bones and shred meat. Discard bones, or freeze them for stock. Return meat to slow cooker. Stir in chard, wild rice, salt, pepper, and zucchini. Cover and cook on low about 1 hour, until rice is tender. Discard thyme sprigs. Stir in lemon juice to taste. Serve.
Celiac.com 05/06/2017 - Want a great gluten-free dinner idea that's tasty and ridiculously easy to make? This recipe for honey-glazed garlic chicken is just what you've been looking for. Just toss the chicken into the slow-cooker, blend the ingredients, pour over the chicken, and turn it on. Come back later, and dinner is ready to go. Serve over rice or gluten-free pasta, and add your favorite side for a delicious dinner. Ingredients: 6 skinless, boneless chicken thighs ½ cup ketchup ½ cup gluten-free soy sauce 3 tablespoons honey 3 cloves garlic, minced 1 teaspoon dried basil Directions: Arrange chicken thighs in the slow cooker. Whisk soy sauce, ketchup, honey, garlic, and basil together in a bowl. Pour over the chicken. Cook on low for 6 hours. Serve with rice, or your favorite gluten-free pasta.
Jefferson Adams posted an article in Gluten-Free American, British/UK RecipesCeliac.com 04/19/2016 - Blackened Redfish is a Cajun classic that can also be prepared quite nicely with the much easier to find Tilapia. This recipe delivers a tasty, flavorful version of blackened fish that pairs well with slow cooked red beans and rice. It's easy to make at the end of a long day. Just cook the fish and rice, and serve up the beans. Blackened Fish Ingredients: 4 tilapia fillets 1 cup long-grain white rice 2 cups fresh flat-leaf Italian parsley 1 teaspoon grated lemon zest 3 tablespoons olive oil 3 tablespoons paprika ¾ teaspoon garlic powder ¾ teaspoon dried thyme ¼ teaspoon cayenne pepper 2 tablespoons fresh lemon juice Kosher salt and pepper Lemon Wedges Directions: Cook the rice according to package directions. Meanwhile, in a food processor, pulse the parsley, lemon zest, 2 tablespoons oil, and 1/4 teaspoon each salt and pepper until finely chopped; set aside. In a small bowl, stir together the paprika, garlic powder, thyme, cayenne, ½ teaspoon salt, and ¼ teaspoon pepper. Brush the lemon juice over the fish, then coat in the spice mixture. Heat the remaining tablespoon oil in a large skillet over medium heat. Cook the fish in two batches, adding extra oil if necessary, until the fish is beginning to blacken and is opaque throughout, 2 to 3 minutes per side. Fluff the rice with a fork and fold in the parsley mixture. Serve with the fish and lemon wedges, if desired. Slow Cooked Red Beans and Rice Ingredients: 1 pound andouille sausage, sliced into rounds 1 large sweet onion, chopped 1 green bell pepper, chopped 1-2 tablespoon gluten-free red pepper sauce, to taste (optional) 8 cloves garlic, chopped 1 teaspoon ground black pepper 1 teaspoon Creole seasoning, or to taste 6 fresh basil leaves, chopped 1 ham hock 4 cups cooked rice Place the beans and water into a slow cooker. Heat a skillet over medium-high heat. Brown the sausage in the skillet; remove from the skillet with a slotted spoon and transfer to the slow cooker. Reserve drippings. Add onion, green pepper, red pepper sauce and garlic to the drippings; cook and stir until tender, about 5 minutes. Transfer everything from the skillet to the slow cooker. Season the mixture with pepper and Creole seasoning. Add the fresh basil leaves and ham hock. Cover and cook on low for about 8 hours, until beans are tender. Cook until beans reach a creamy texture.
By Jessica Mahood , M.S. Bacteriology Celiac.com 09/28/2004 - A very good question: what is gliadin and why does it survive a bath in hot oil? I am a little hesitant to answer because I am not a protein chemist who specializes in such things. However, I was a bacteriologist with many years of exposure to biochemical concepts, so Im probably better equipped than most to give this a go. First of all, a protein primer: As someone mentioned, proteins are made up of building blocks. We generally call these amino acids. Sometimes amino acids are represented in the scientific literature as a single letter--you will see something like PQQLL (pay attention to this because it will come up again later). Each of those letters stands for an amino acid that is linked to the next. So, imagine the amino acids to be beads in a necklace. This configuration--the beads of amino acids connected in the necklace--is called the primary structure. Now, imagine this necklace to be twisted around itself in some fashion. This is generally known as the secondary structure of the protein and often looks like a helix. Next, take that twisted necklace and bend it around into a 3-D blob. This is known as the tertiary structure. If you were to take several different necklaces compressed into this tertiary structure and combine them, you would have a quaternary structure. So, there are four basic levels of protein structure, primary through quaternary. Of course, the actual chemistry is a bit more complicated, because many amino acids have a chemical charge to them that can influence how they respond to their neighbors, or to the outside environment. Think of a magnet--like repels like, attracts opposite. If they are attracted or repelled, its going to effect the ultimate structure of that protein. Amino acids, as molecules, are also different sizes. One amino acid may be like a small bead that fits easily between the others, while the next amino acid could be huge and practically hanging off of the necklace. Imagine this as a lump in our necklace that prohibits it from fitting neatly against another necklace in our blob. There is also the fact that not all proteins have all four of the levels of structure. Some proteins simply exist as a secondary structure or tertiary structure. So, there are many different types of protein structures in nature. Often times, these depend on the job of the protein. Hopefully I havent thoroughly confused you by now. Suffice it to say that there are many factors involved in determining the properties of a certain protein. So much so that there are actually a set series of tests that scientists use to classify proteins. It is a very complex discipline. Now, back to your original question. Proteins cannot be killed, per se, as they are not alive. HOWEVER, they can be damaged or destroyed. This is a process that is called denaturation. Denaturation can be irreversible, such as when you burn something to a crisp. Its as if you melted the strand of that necklace and all of the shapes that it made were lost. Denaturation can also be somewhat temporary. You denature your hair, to some extent, when you use a curling iron. You are slightly unraveling a higher structure of the hair protein, but it can be righted over time (unless the curling iron is too hot!). The ease with which a protein denatures depends on many things. Think back to our necklace. If we have, say, five necklaces clustered together to form a single protein, it would probably take a lot of chemical disruption to fully destroy that protein. However, if we had one tiny necklace twisted up slightly, it would be a lot less work to break it apart. There are many other factors involved in this--the size and charge of the beads, for example. Gliadin is a fragment of the protein gluten. Gliadin is NOT a single amino acid. Gliadin is simply a subset of a larger protein. Think of it as one necklace within a jumble of many. According to a Stanford research website (http://www.friedli.com/research/PhD/Predict/discuss.html), gluten has the basic structure of: MKTFLILALLAIVATTATTAVRVPVPQLQPQNPSQQQPQ EQVPLVQQQQFLGQQQPFPPQQPYPQPQPFPSQQPYLQLQ PFLQPQLPYSQPQPFRPQQPYPQPQPQYSQPQQPISQQQQ QQQQQQQQQQQQQQQIIQQILQQQLIPCMDVVLQQHNIV HGKSQVLQQSTYQLLQELCCQHLWQIPEQSQCQAIHNVVH AIILHQQQKQQQQPSSQVSFQQPLQQYPLGQGSFRPSQQ NPQAQGSVQPQQLPQFEEIRNLARK What do these letters mean? Again, they are amino acids. Each one of those letters stands for an amino acid. Its like a code. If the same letter is used, the same amino acid is in those two parts. Within that larger sequence, you see: RPQQPYPQPQPQ This smaller list of letters is the amino acid code for gliadin. So just for a start, in denaturing our gliadin, we have to destroy all of the rest of the gluten protein that is around it. The next issue is that this sequence contains the letter Q several times. This letter Q represents the amino acid glutamine. This is probably what the person meant when they said that gliadin was an amino acid. They were most likely thinking of glutamine. In any case, as far as amino acids go, glutamine is fairly large and pretty hearty. At this point in time, go to the following website: http://www.chemie.fu-berlin.de/chemistry/bio/aminoacid/glutamin_en.html Look at the picture of glutamine next to the name at the top--it looks like a couple of groups of letters connected by black lines. If you look to the far left, you see the letters H2N. A certain chemical process in the body changes that H2N into a different chemical group. This is called deamidation, and you hear about it a lot in reference to the Celiac response. It is the deamidated protein within the gliadin fragment of the gluten protein that is believed to be the big trigger for the antibody response that causes damage. What a mouthful, eh? Back to gliadin and hot oil, the original question. Okay, so now we know that proteins are pretty complicated. They can have big structures and lots of chemical interactions. Gluten is such a protein. The gliadin fragment of the gluten protein is tough to get to. You must also destroy the properties of the amino acids in the gliadin fragment to truly nullify the immune-irritating properties of gliadin to Celiacs. So, for various chemical reasons, gliadin is not easy to denature. According to that Stanford website (http://www.friedli.com/research/PhD/chapter8.html), gliadin is tough stuff. Many changes made to the protein are reversible. Researchers are still exploring the properties of gliadin and trying to find a way to use the molecules interactions to stop the Celiac response. It gives me a hope. For now, we have to resign ourselves to being suspicious of those soupy vats of oil in the back of bars and restaurants.