Guest guest Posted November 14, 2002 Report Share Posted November 14, 2002 Hi Suze, I don't know how long it lasts because I always cook mine, and eat the leftovers over the week, but I wonder what the lemon juice will do to it over long periods of time. It seems that after a couple hours it almost sort of " cooks " it, in that the color starts turning in the outside from reddish to a gray, cooked color, and it certainly tenderizes it and whatnot. I wonder what will happen if that process is allowed to continue over several days. I also wonder, as an aside, whether anything is happening to the proteins that decrease the " raw " value of it. (If anyone knows please chirp in). So anyway, I'd be interested to hear the progress of how your liver looks, feels, tastes, after sitting in the lemon juice for so long, if you wouldn't mind giving an update. Chris Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 14, 2002 Report Share Posted November 14, 2002 In a message dated 11/14/02 4:21:14 PM Eastern Standard Time, darkstar@... writes: > The secondary etc. structure of proteins is partly influenced by H+ > bonds which will be affected by pH. So the acid will denature > proteins to a certain extent, depending on the protein and the pH. > Same with high salt. They may lose their shape and function, maybe > irreversibly, again depending on he individual protein, pH etc. > Heat also affects the H+ bonds and denatures proteins so some overlap > with cooking, although I wouldn't call it the same (especially for > higher temps.) > Darkstar (Martha, right?), Are you on an all-raw diet? If so, do you consider lacto-fermenting, marinading in acidic solutions, and other such processes, to be a violation of the all-raw diet? Do you consider raw foods that haven't come into contact with acids to be superior in health value? Do such things denature all protein equally, or are enzymes left in tact while other structural proteins are damaged, etc? Thank you for any help, Chris Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 14, 2002 Report Share Posted November 14, 2002 >I > also wonder, as an aside, whether anything is happening to the proteins that > decrease the " raw " value of it. (If anyone knows please chirp in). > The secondary etc. structure of proteins is partly influenced by H+ bonds which will be affected by pH. So the acid will denature proteins to a certain extent, depending on the protein and the pH. Same with high salt. They may lose their shape and function, maybe irreversibly, again depending on he individual protein, pH etc. Heat also affects the H+ bonds and denatures proteins so some overlap with cooking, although I wouldn't call it the same (especially for higher temps.) Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 14, 2002 Report Share Posted November 14, 2002 >I > also wonder, as an aside, whether anything is happening to the proteins that > decrease the " raw " value of it. (If anyone knows please chirp in). > The secondary etc. structure of proteins is partly influenced by H+ bonds which will be affected by pH. So the acid will denature proteins to a certain extent, depending on the protein and the pH. ---------->martha, can you tell me what you mean by " denature " ? what specifically happens during 'denaturing?' Same with high salt. They may lose their shape and function, maybe irreversibly, again depending on he individual protein, pH etc. Heat also affects the H+ bonds and denatures proteins so some overlap with cooking, although I wouldn't call it the same (especially for higher temps.) ------->heat also affects heat-labile vitamins, but i don't imagine that lemon juice has the same affect? so, aside from the proteins, wouldn't there be components that are more intact in the lemon soaked raw liver as opposed to cooked liver? Funny, i used to soak my dogs' raw meat/organs/bone in ACV. I'd just defrost a big batch, pour some raw ACV on, and take out portions throughout the week. i never felt like i was 'cooking' their raw food. I thought the ACV would mainly 'pre-digest' it to some extent in the way that stomach acid helps prepare proteins and fats for digestion in the small intestine. in regards to chris' question: <<also wonder, as an aside, whether anything is happening to the proteins that > decrease the " raw " value of it. >> ----->i don't know, but lemon juice and stomach acid (in healthy humans) is about the same pH - around 2-3 (also might depend on what's eaten). So if lemon juice *decreases* the value of raw liver, then so to would stomach acid, based in terms of pH. however, maybe the lemon juice could decrease the value of it *over time..?* hopefully, it won't be sitting *in my stomach* for a week! Suze Fisher Lapdog Design, Inc. Web Design & Development http://members.bellatlantic.net/~vze3shjg/ mailto:s.fisher22@... Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 14, 2002 Report Share Posted November 14, 2002 In a message dated 11/14/02 11:18:57 PM Eastern Standard Time, s.fisher22@... writes: > " denature " *sounds* > like a bad thing, but it's not necessarily so, as far as i understand it, > and actually may *increase* digestibility. in fact, isn't > protein*digestion* > itself a process of 'denaturing' proteins? Well, something in raw animal foods increases digestibility over cooked. I would have thought that it's proteins (enzymes) retaining their " function. " Lacto-fermenting and marinading seems to increase the digestibility of everything, but cooking certainly doesn't, only in certain foods, an in my experience, invariably _not_ in animal foods. And something in raw meat is giving lots of people lots of energy, and has been helping my immune system a lot, as someone else on this list also mentions. If all the enzymes are destroyed as Martha suspects and if denaturing the proteins is better, not worse, than I'm at a loss to explain the increased energy and immune system support from raw animal foods. Not that I would know better, just that there must be _something_ to explain it. Chris Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 In a message dated 11/14/02 11:51:35 PM Eastern Standard Time, dkemnitz2000@... writes: > And when I GOT to that > land grant institution I Got the answer. Dennis > Just curious what institution that is. UMass Amherst is a land grant institution, where I'm at. I wish I majored in biochem instead of history ;-) Chris Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 > > ---------->martha, can you tell me what you mean by " denature " ? what > specifically happens during 'denaturing?' > Here's definition from Molec Bio of Cell - denaturation: dramatic change in conformation of a protein or nucleic acid caused by heating or by exposure to chemicals and usually resulting in loss of biological function. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 ---Martha, enzymes probably denature, generally speaking, from heat and acidification too, right? Even making yogurt with L. acidophilus will cause the milk proteins and enzymes, most likely, to denature. In @y..., " darkstardog " <darkstar@p...> wrote: > > > > > ---------->martha, can you tell me what you mean by " denature " ? what > > specifically happens during 'denaturing?' > > > Here's definition from Molec Bio of Cell - > denaturation: dramatic change in conformation of a protein or nucleic > acid caused by heating or by exposure to chemicals and usually > resulting in loss of biological function. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 > --- In @y..., " Suze Fisher " <s.fisher22@v...> wrote: > > > > ---------->martha, can you tell me what you mean by " denature " ? what> > specifically happens during 'denaturing?' > > From ancient edition of Biochemistry text (Lehninger): Denaturation: Most protein molecules retain their biological activity or capacity to function only within a very limited range of temperatures and pH. Exposure of protein molecules to extremes of pH or temperature causes them to undergo a change known as denaturation, in which the msot visible effect in globular proteins is a decrease in solubility. Most proteins undergo denaturation when heated over 50 to 60 degrees C; some also denature when cooled below 10 to 15 degrees C. the formation of an insoluble white coagulum during the heating of egg white is a good example of denaturation. Denaturation also causes proteins to lose their characteristic biological activity. For example, when enzymes are heated their ability to catalyze a specific biological reaction is ususally lost. Since the covalent bonds in the peptide backbone of proteins are not broken during denaturation, it has been concluded that denaturation is due to the unfolding of the characterisitc folded structure of the polypeptide chain in the native protein molecule. In the denaturaed state, teh polypeptide chains are randomly and irregularly looped or coiled and the conformation of any given chain may change with time. .... (renaturation: returning protein to original conditions of temp and pH may return it to previous configuration with return of function. But not necessarily. Also, " For this reason, the renaturation of many proteins gives the appearance of being irreversible, because refolding to the native state is often a very slow process. " depends on the native structure.) Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 > Are you on an all-raw diet? If so, do you consider > lacto-fermenting, > marinading in acidic solutions, and other such > processes, to be a violation > of the all-raw diet? I'm not on a raw food diet and I'm ignorant of how raw food people would think about the question, so I can't help. > Do you consider raw foods that haven't come into contact with > > acids to be superior in health value? As Suze said, the foods are going to come into contact with stomach acid anyway, which may be even more acidic than lemon juice or vinegar. So I don't don't think it makes a difference. But I don't have a good answer. > Do such things denature > all protein equally, or are enzymes left > intact while other structural proteins are damaged, etc? I'd guess that enzymes were more vulnerable. But again it depends on the specific protein. Obviously the pepsin enzyme is functional at the low stomach pH. And as far as heat goes, there are bacteria that live in the steam vents at the bottom of the ocean and some of those enzymes can function almost to boiling if I understand correctly. I think most enzymes would be denatured, but I think I've read that some like amylase can renature in neutral pH in the intestine. (Not sure about that; I don't think I read it in a reliable source.) But I think I've read that most enzymes in food are denatured irreversibly in the stomach. (Again, not positive.) (As I've said before in various places, so far I'm not a believer in the importance of enzymes in raw food; although they may do some digestion in the stomach before they are exposed to too low a concentration of acid, I have yet to see any good evidence for how much digestion they actually do or whether there are any health benefits. (This doesn't mean there aren't any.) AS for other ingredients in foods like vitamins, that Suze brought up - I don't know - I was just responding to the point about the proteins. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 > - I don't know - I was just responding to the point about the > proteins. Goodness, that was a post full of negativity and uncertainty. Just the way I feel today. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 --- Martha I hope tomorrow is more wonderful for you. I sure enjoy your chemistry input. Dennis In @y..., " darkstardog " <darkstar@p...> wrote: > > > - I don't know - I was just responding to the point about the > > proteins. > > Goodness, that was a post full of negativity and uncertainty. Just > the way I feel today. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 >>>>Here's definition from Molec Bio of Cell - denaturation: dramatic change in conformation of a protein or nucleic acid caused by heating or by exposure to chemicals and usually resulting in loss of biological function. >>>>>From ancient edition of Biochemistry text (Lehninger): Denaturation also causes proteins to lose their characteristic biological activity. For example, when enzymes are heated their ability to catalyze a specific biological reaction is ususally lost. Since the covalent bonds in the peptide backbone of proteins are not broken during denaturation, it has been concluded that denaturation is due to the unfolding of the characterisitc folded structure of the polypeptide chain in the native protein molecule. In the denaturaed state, teh polypeptide chains are randomly and irregularly looped or coiled and the conformation of any given chain may change with time. ----------->martha, thanks for looking those up :-) this is what I understand from this; extremes in pH (as well as heat) UNfolds polypeptide chains. the protein cannot carry out it's function when it's unfolded. i checked molec. biology of the cell, and on page 489 they discuss denaturing proteins with detergents for *study* purposes. and they mention the loss of function. Since i'm not *studying* the protein in my liver (just eating it), I'm not sure if need it to carry out any functions? After an animal dies, do the proteins in it's tissue continue to *function* in some way? OK, now applying the above descriptions to the *digestibility* of raw liver soaked in lemon juice, I'm thinking it would improve digestibility because the polypeptides are unfolding and that would increase surface area for digestive enzymes (including pepsin in the stomach) to work on. right? I don't see where the acidic pH of lemon juice would do anything *harmful* to the proteins (unless i'm not understanding this well). " denature " *sounds* like a bad thing, but it's not necessarily so, as far as i understand it, and actually may *increase* digestibility. in fact, isn't protein*digestion* itself a process of 'denaturing' proteins? Relatedly, I've also read that HCl softens connective tissue. that's what marinades do as well, and my lemon soaked liver is certainly much softer than it was prior to soaking. If I'm not misunderstanding what denaturing is, then this all suggests that lemon soaked raw liver would be easier to digest than plain ol' raw liver..? (interestingly, NT recommends soaking liver in lemon juice before cooking -*double* denaturing! LOL) p.s. i think one of the biggest benefits of raw over *cooked* is the lipids, especially anything with a relatively high PUFA content. p.p.s. i wonder if meat/organs have 'self' digesting enzymes like *raw* milk has lactase (and pasteurized doesn't) and some sourdough yeasts contain *phytase* that digest phytate in the flour? Do most foods contain self-digestiong enzymes? darnit! one question begets 20. <g> Suze Fisher Lapdog Design, Inc. Web Design & Development http://members.bellatlantic.net/~vze3shjg/ mailto:s.fisher22@... Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 >>>>>I'd guess that enzymes were more vulnerable. But again it depends on the specific protein. Obviously the pepsin enzyme is functional at the low stomach pH. ------->hmmmm...that's a good point. i've also read that a pH of 1.5-2 is *required* for converting pepsinogen to pepsin (in the stomach). >>>>I think most enzymes would be denatured, but I think I've read that some like amylase can renature in neutral pH in the intestine. (Not sure about that; I don't think I read it in a reliable source.) ---------------->yes, I've read it too. That means that salivary amylase is temporarily 'neutralized' while in the stomach, then 're-activated' when it gets to the duodenum. i've read that different enzymes require specific pHs in order to function, so from that perspective, it would make sense. OTOH, i'm not sure why it would be necessary to 're-activate' since pancreatic amylase is brought into the intestines to digest carbs. i don't know enough about the specifics of what goes on in the duodenum to know if the 're-activation' makes sense or not. though. Suze Fisher Lapdog Design, Inc. Web Design & Development http://members.bellatlantic.net/~vze3shjg/ mailto:s.fisher22@... Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 ---How about some humor, Martha? Check out message 13240 at groups/group/pasturepoultry/messages. It's a chicken and egg story and it's not about nor did it happen to Dorothy. Dennis In @y..., " darkstardog " <darkstar@p...> wrote: > > > - I don't know - I was just responding to the point about the > > proteins. > > Goodness, that was a post full of negativity and uncertainty. Just > the way I feel today. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 ---I wrote once or more about biochemical reactions undertaking many steps to get to the end product and their reversibility (kinetics,etc). And biochem is even more aewsome(complex!). So those intermediates may be beneficial or may be empty calories so to speak, in some ways like phytates are spoken of by NT folks. Biochemistry seems to me an exciting and interesting field but I only made it thru general bio. (like one 5 or 4 hour course). Too late to study that complicated stuff nowadays so anyway that's my update. Denis In @y..., ChrisMasterjohn@a... wrote: > In a message dated 11/14/02 11:18:57 PM Eastern Standard Time, > s.fisher22@v... writes: > > > > " denature " *sounds* > > like a bad thing, but it's not necessarily so, as far as i understand it, > > and actually may *increase* digestibility. in fact, isn't > > protein*digestion* > > itself a process of 'denaturing' proteins? > > Well, something in raw animal foods increases digestibility over cooked. I > would have thought that it's proteins (enzymes) retaining their " function. " > Lacto-fermenting and marinading seems to increase the digestibility of > everything, but cooking certainly doesn't, only in certain foods, an in my > experience, invariably _not_ in animal foods. > > And something in raw meat is giving lots of people lots of energy, and has > been helping my immune system a lot, as someone else on this list also > mentions. > > If all the enzymes are destroyed as Martha suspects and if denaturing the > proteins is better, not worse, than I'm at a loss to explain the increased > energy and immune system support from raw animal foods. > > Not that I would know better, just that there must be _something_ to explain > it. > > Chris > > > Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 --- By def'n when a protein reaches it's isoelectric point it precipitates(turns into a solid). There's probably exceptions BUT anyway. I remember this because I always (not totally) wondered what made an egg harden when cooked on the stove. And when I GOT to that land grant institution I Got the answer. Dennis In @y..., " dkemnitz2000 " <dkemnitz2000@y...> wrote: > ---I wrote once or more about biochemical reactions undertaking many > steps to get to the end product and their reversibility > (> > <><><><<><><><><><><><<<>clipped by Dennis<><<><<><<> > > > " denature " *sounds* > > > like a bad thing, but it's not necessarily so, as far as i > understand it, > > > and actually may *increase* digestibility. in fact, isn't > > > protein*digestion* > > > itself a process of 'denaturing' proteins? > > > Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 --- By def'n when a protein reaches it's isoelectric point it precipitates(turns into a solid). There's probably exceptions BUT anyway. I remember this because I always (not totally) wondered what made an egg harden when cooked on the stove. And when I GOT to that land grant institution I Got the answer. Dennis In @y..., " dkemnitz2000 " <dkemnitz2000@y...> wrote: > ---I wrote once or more about biochemical reactions undertaking many > steps to get to the end product and their reversibility > (> > <><><><<><><><><><><><<<>clipped by Dennis<><<><<><<> > > > " denature " *sounds* > > > like a bad thing, but it's not necessarily so, as far as i > understand it, > > > and actually may *increase* digestibility. in fact, isn't > > > protein*digestion* > > > itself a process of 'denaturing' proteins? > > > Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 ---If you can remember all those dates(history) you would be a natural at biochemistry. Really, there's lots of memorization in the entry chemistry classes. Have you had chemistry, even a little bit. I graduated at Kansas State 10 years after graduating h.s. class. I'm a Kansas State Wildcat! I took time out after high school to see the world and to get the GI bill. Had to get out of KS, for a while anyway. Any other questions feel free to write. Dennis In @y..., ChrisMasterjohn@a... wrote: > In a message dated 11/14/02 11:51:35 PM Eastern Standard Time, > dkemnitz2000@y... writes: > > > > And when I GOT to that > > land grant institution I Got the answer. Dennis > > > > Just curious what institution that is. UMass Amherst is a land grant > institution, where I'm at. I wish I majored in biochem instead of history > ;-) > > Chris > > > Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 >> > ---------------->yes, I've read it too. That means that salivary amylase is> temporarily 'neutralized' while in the stomach, then 're-activated' when it> gets to the duodenum. i've read that different enzymes require specific pHs > in order to function, so from that perspective, it would make sense. OTOH,> i'm not sure why it would be necessary to 're-activate' since pancreatic> amylase is brought into the intestines to digest carbs. i don't know enough> about the specifics of what goes on in the duodenum to know if the> 're-activation' makes sense or not. though. > It's not that the body is taking a specific action to reactivate or renature the salivary amylase. If it happened, it would happen automatically as a result of the return to a neutral pH. The molecule would tend to automatically refold into its most stable formation at that pH. The trouble is, with a complex molecule it might be hard to get back to that point. It's kind of like a jacket with lots of velcro fasteners - you don't want the neck velcro stuck to the waist velcro. Some molecules have helper molecules that help to fold them into shape as they are being formed initially (chaperones?). Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 --- In @y..., " dkemnitz2000 " <dkemnitz2000@y...> wrote: > --- Martha I hope tomorrow is more wonderful for you. I sure enjoy > your chemistry input. Dennis > Thanks, Dennis! Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 > > After an> animal dies, do the proteins in it's tissue continue to *function* in some> way? Yes, I think some proteases (not all) are able to function, depending on temp, pH and Ca++ levels - ageing of meats and the relaxing of rigor mortis, for example. (Enzymes requiring energy, structural integrity of the cell, etc, would not.) How much digestion actually goes on in the stomach (37 degrees) before the food is made too acidic - that I don't know. > > OK, now applying the above descriptions to the *digestibility* of raw liver> soaked in lemon juice, I'm thinking it would improve digestibility because> the polypeptides are unfolding and that would increase surface area for> digestive enzymes (including pepsin in the stomach) to work on. Seems like yes and no - maybe some areas more accessible, others less if some of the proteins clump up - I'm out of my depth. Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 In a message dated 11/15/02 12:23:00 AM Eastern Standard Time, dkemnitz2000@... writes: > ---If you can remember all those dates(history) you would be a > natural at biochemistry. Really, there's lots of memorization in the > entry chemistry classes. Have you had chemistry, even a little bit. > I graduated at Kansas State 10 years after graduating h.s. class. > I'm a Kansas State Wildcat! I took time out after high school to see > the world and to get the GI bill. Had to get out of KS, for a while > anyway. Any other questions feel free to write. I've never taken an official chem class. I did have a love for the biochem section of biology when I took it, and I must have had a knack for it or something because my teacher and the head tutor were begging me to take biochem, for whatever reason. It was funny, I was tutoring that class at the same time I was taking it. I've always been into science, but I took history because back when I was an anarchist I thought being a social studies teacher was the best way I could make my personal contribution to the revolution. I'm not sure what I'm going to do now. I was toying with the idea of taking pre-med classes and try to get into med school, picking up a second major in biochem, and some other ideas, but I don't know if it's worth it. I think I just want to move to Maine or Vermont, buy a big hunk of land, and start farming it. My experience with college is that it's mostly a waste of time. If I were an english major I'd have valued having peer critique, writing workshops, etc, but you don't need college for those. If I were a science major I'd have valued having easy access to laboratories, but yeah, labs are fun, but I don't know if I want to spend another two years worth of time and money just to spend a few weeks in one-- I could just pick up a biochem book and read it. Ahh, well, I have plenty of time. Chris Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 In a message dated 11/15/02 7:55:31 AM Eastern Standard Time, s.fisher22@... writes: > (as an interesting aside, they mention that casein is highly resistant to > heat denaturing.) > That's interesting because of the charges that pasterization causes protein-shape changes that contribute to autoimmune disorders. Then again, what is, in relativity, " high resistance " ? Meat usually gets heated to 170-180, and I'm sure the denaturation takes place before that, so casein might have particularly high resistance but maybe that has no value in practicality... or maybe it does. > after all this, i'm still not sure if soaking my liver in lemon has a net > positive or negative effect on it. LOL but i *am* sure that it's a heck of > a > lot more palitable after it's been swimming in lemon juice! (even more so > than *cooked* liver, imo.) Lol, I'll have to try it some time. Lemon juice sure does help out even cooking it though. Chris Quote Link to comment Share on other sites More sharing options...
Guest guest Posted November 15, 2002 Report Share Posted November 15, 2002 >>>>If all the enzymes are destroyed as Martha suspects and if denaturing the proteins is better, not worse, than I'm at a loss to explain the increased energy and immune system support from raw animal foods. --------->well, two ways that *raw* animal foods are probably healthier than cooked, is that the fats are *not* exposed to heat (and thus less prone to oxidation) and the heat-labile vits are not destroyed by heat. so theoretically you're getting less damaged fats and more vits. Here's a lecture on protein denaturation from Ohio State Food Science dept: http://class.fst.ohio-state.edu/FST605/lectures/Lect11.html This goes pretty indepth in regards to the different forms of denaturing proteins. Here's an excerpt re: *pH* denaturing (there's a different section on *thermal* denaturing): <<If the pH is lowered far below the isoelectric point, the protein will lose its negative and contain only positive charges. The like charges will repel each other and prevent the protein from aggregating as readily. In areas of large charge density, the intramolecular repulsion may be great enough to cause unfolding of the protein. This will have an effect similar to that of mild heat treatment on the protein structure. In some cases the unfolding may be extensive enough to expose hydrophobic groups and cause irreversible aggregation. Until this occurs such unfolding will be largely reversible.>> <<Some proteins contain acid labile groups and even relatively mild acid treatment may cause irreversible loss of function. This generally results from the breaking of specific covalent bonds and thus should be considered separately from denaturation. Exposure to strong enough acid at elevated temperatures will first release amide nitrogen from glutamine and asparagine groups and eventually lead to hydrolysis of peptide bonds.>> ---->so, it seems they're saying that low pH has a similar effect on protein as 'mild' heat. but, they go on to say that acid may cause hydrolyis of peptide bonds, which is a kind of 'pre-digestion' as far as i understand it. The main concern with denaturing protein, that i got from this lecture, is the loss of solubility (which would make it less digestible i *think*). They described how *heat* can decrease solubility of protein, but i didn't see mention of acid pH causing loss of solubility. (as an interesting aside, they mention that casein is highly resistant to heat denaturing.) after all this, i'm still not sure if soaking my liver in lemon has a net positive or negative effect on it. LOL but i *am* sure that it's a heck of a lot more palitable after it's been swimming in lemon juice! (even more so than *cooked* liver, imo.) Suze Fisher Lapdog Design, Inc. Web Design & Development http://members.bellatlantic.net/~vze3shjg/ mailto:s.fisher22@... Quote Link to comment Share on other sites More sharing options...
Recommended Posts
Join the conversation
You are posting as a guest. If you have an account, sign in now to post with your account.
Note: Your post will require moderator approval before it will be visible.