Tasting Food With Your Nose
Did you know we humans experience only four fundamental tastes? Before reading much further, pause and see if you are able to name them. Some scientists allege the existence of a fifth taste called "umami", which they perceive as "savory". As we make distinctions with the unique characteristics of tastes, we perceive flavors. Nothing new here, but did you know that the way a food smells actually accounts for more than 70 percent of the flavor we perceive? Why is the sense of taste so much less complex? Taste merely makes distinctions in the quality of food (or any other material) we have already selected and placed into our mouths. Our four fundamental tastes are sweet, salty, bitter, and sour. In primitive man, a keen sense of smell was vital for successfully hunting food - often under dangerous conditions - and his ability to quickly detect and recognize thousands of odors became advanced. He could qualify it later, using his much less complex sensation of taste. Of course food had to taste good, simply to be palatable.
Odors and aromas of foods need volatile compounds (organic chemicals that have a high vapor pressure at ordinary, room-temperature conditions) to reach our nasal cavities, and the aroma of hot food is usually the only encouragement we need to straighten up and be seated at the dining table. That`s fine for Snagman`s Hungarian Csabaii, but what about Uwanna`s cold Alysandra salami? When the temperature of food drops, very little vapor is released. Accordingly, most cold food does not have much odor, not to mention taste. Thus, a problem occurs when we prepare or eat cold food - how do we keep it interesting? How does Wally soup-up his sensational salami so it attracts a little attention? One solution is to use particularly pungent flavorings such as garlic or onion. Other foods may use citrus for a little potency.
The best answer is to spotlight the four basic tastes of sweet, salty, bitter, and sour. Many sausage makers select strong-smelling seasonings to heighten taste, but because acidity may be detected at low temperatures, the development of lactobacilli becomes most essential. In some cultures, vinegar is sometimes used as it is in chorizo and similar sausages. It`s also found in such cold recipes for pickles, soups, dips, and dressings.
What about our sweet tooth? We focus upon the sweetness of cold desserts such as ice cream by commonly adding hefty quantities of sugar. Only our sensitivity to salt remains somewhat uniform whenever tasting both cold and warm foods, and we usually add comparable quantities to each. Experienced cooks often check cold foods just before serving them to see if they require more salt. Experienced home sausage makers often cook up a quick sample and taste it before the batch is stuffed into casings.
Another consideration is an introduction of contrasting flavors. For instance, sprinkling salt on cold watermelon or pineapple emphasizes their sweetness by providing a distinctive counterbalance. Can you think of any application in sausage making where this might occur?
We have almost 10,000 taste buds inside our mouths and in general, females have more tastebuds than males. Taste buds sensing salty and sweet flavors are located near the front of the tongue while those identifying sour flavors line its sides. Bitter flavors are identified at the very back of the tongue. Our sense of taste is the weakest of the five senses and as we grow older, our taste buds become less sensitive. Many older people are more likely to eat foods they once thought were too strong - including Ross` chicken!
It may be fun to really learn how to taste the sausages you make. Why not take a new approach to savoring your hard work? Begin by tasting any other food - soup for instance. Be sure to check the temperature before placing a scalding, savory, soup sample into your mouth. Juggling a spoonful of steaming, 210-degree, Crusty`s "chicken-noodle ambush" inside your mouth will completely take your mind away from your immediate objective. Smell the sample first. Leave your nasal passages open and close your mouth. Close your eyes and move it all about your mouth or swirl it around a little if tasting liquid. Notice which taste buds react most as you individually evaluate sweetness, saltiness, bitterness, or sourness. Concentrate and appraise each of the four tastes you were born with. Through experience, many chefs develop a talent for correcting their dishes by using their "mind`s eye" - imagining the effect of added seasonings upon their final effort. I`ve seen old time sausage makers taste, squint, rub their whiskers, reach inside the grub box, then add just exactly the right amount of one thing or another to the mixture, "seasonin` the blend" perfectly. These same ol` pros usually stick to the basics - salt, sugar, pepper, and perhaps a "signature spice" to make the best sausage. Most have learned that too much spice or too many spices are simply not necessary to create sensational sausage.
Saddlebum Savvy And Recipe Rescues
As we cook, it becomes important to frequently taste food to avoid the use of too much seasoning or adding it too soon. Removing a spice, herb, or seasoning cannot be done once it has been added. By the way, herbs come from plants - spices from seeds. Some just naturally blend well used together. For example, equal amounts of basil and oregano, with half as much thyme, make a first-rate choice seasoning for thousands of recipes! Some herbs and spices should be used in moderation. Rosemary, ginger, sage, and tarragon have comparatively strong flavors and as a general rule should be used sparingly. On the other hand, some spices or herbs, such as dill, should be used by themselves. Others are added to food liberally, only following the cooking process. This is especially true whenever deep-frying food. Never add spices or herbs to hot oil.
Beginners, believing they may "neutralize" the sweetness of sugar by adding more salt, or curb the taste of salt by using more sugar, have much to learn. Yet, occasionally, some dishes may be adjusted or "pulled up" using a bit of "western saddlebum savvy". The following remedies are not foolproof yet may help if a situation is not too grim.
If a food is too spicy, try adding some sweetness or creaminess. Too sweet? Don`t add salt! Try adding something sour or spicy hot. If a food is too bland, try adding salt or some spicy heat. If it`s too salty, don`t add sugar! As an alternative, try adding something sour. If something is just too harsh, you may try adding a touch of something sweet, and if your cooking just needs a kick in the fanny because it lacks depth, charge it up using something acid or aromatic near the end of cooking - perhaps vinegar or an ingredient with just a bit of spicy heat in it.
I hope your taste buds just reach up and tickle yer` tonsils!
Best Wishes,
Chuckwagon
Tasting Food Using Your Nose
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Chuckwagon
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Tasting Food Using Your Nose
If it looks like a duck, walks like a duck, and quacks like a duck, it probably needs more time on the grill! 
Re: Tasting Food Using Your Nose
Regarding my marinating problem, avoiding using acid because it makes the sausage crumbly, what are your thoughts?Chuckwagon wrote:Tasting Food With Your Nose
charge it up using something acid or aromatic near the end of cooking - perhaps vinegar or an ingredient with just a bit of spicy heat in it.
Perhaps one way would be to marinate using everything but the acid components, then cooking the sausage, then using a second marinade with the acid components. For my usual mix, I'd have to stuff sausage with rosemary-infused olive oil plus the usual salt/pepper/etc, stuff, cure, cook, then add the vinegar later.
Experience - the ability to instantly recognize a mistake when you make it again.
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Chuckwagon
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Thanks Red,
I don't mean to come off so much as a teacher but old habits die hard. (I taught at a university for 20 years). Nice of you to mention my post and I hope you start tasting food with your nose! And don't forget to close your eyes too!
Best Wishes,
Chuckwagon
I don't mean to come off so much as a teacher but old habits die hard. (I taught at a university for 20 years). Nice of you to mention my post and I hope you start tasting food with your nose! And don't forget to close your eyes too!
Best Wishes,
Chuckwagon
If it looks like a duck, walks like a duck, and quacks like a duck, it probably needs more time on the grill!
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Chuckwagon
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Hi Duck, Nice to have you back.
You asked:
The body`s weight is about 15% proteins - large molecules made of hundreds of carbon, hydrogen, oxygen, and nitrogen atoms. Broken down into smaller parts, science identifies specific "amino acids". There are three types of meat proteins:
1. Sarcoplasmic (plasma) water soluble - myoglobin - belongs to this group (gives meat its color)
2. Myofibrillar (contractile) salt soluble - myosin and actin - belongs to this group (water-holding & emulsifying)
3. Stromal (connective) relatively insoluble - collagen and elastin - belong to this group (transmit movement)
Sarcopolasmic proteins are found in intracellular fluid and compose 30% of total muscle protein. They contribute only 20% to binding ability and the isoelectric point of its molecules is low, although they do contribute to tenderization through postmortem glycolysis, effecting a pH change. Sarcopalasmic proteins potentially add flavor contributions from a process known as "protein hydrolysis". Myoglobin consists of a typical amino acid protein concentration responsible for color intensity in meat. It was biologically designed to hold oxygen, and then release it for energy metabolism, so... it binds oxygen somewhat temporarily, dramatically changing meat`s color. Below are a few typical concentrations:
poultry white muscle .05 mg/g
chicken thigh 1.8-2.0 mg/g
turkey thigh 2.5-3.0 mg/g
pork, veal 1.0-3.0 mg/g
beef 4.0-10.0 mg/g
old beef 15.0-20.0 mg/g
mechanically separated meat 0.08-3.0 mg/g
Myofibrillar proteins are called the "contractile" proteins for the way they act upon muscle e.g. rigor mortis. Myofibrillar proteins are composed of 55% myosin - generally considered the single most important because of their long, highly-charged, "filament" molecule that is present in lean muscle. Actin and myosin are primarily responsible for creating the "sticky gel" that holds mixed, comminuted meat together.
Stromal proteins are in connective tissue and are primarily collagen, composing about 20 - 25% total body protein in the skin, sinews, tendons, etc. They are designed to transmit force to hold things together, thus they are generally tough and inert. Stromal proteins are of little or no value in processed meats as they have little binding ability. Further, as an animal ages, its meat becomes tougher due to the stromal protein`s unique make-up of 33% glycine and 10% hydroxyproline - responsible for non-charged or "non-polar" molecules having a minimally low isoelectric point. Stromal protein is generally considered a problem in processed meats and "high collagen meats" are often limited to 15 - 25% maximum, although chopped, ground, powdered collagen which can be dispersed, can be useful in forming a gel when heated. They may also be useful in retaining water and fat.
If sausage is overly mechanically-cut or tumbled, especially with the addition of salt or water, it may have the extraction of two of its myofibrillar proteins (myosin and actin) developed to a point where the structure of the final texture becomes more elastic than that in less-agitated processing. This elasticity may also be perceived as toughness or stiffness in texture. Most often an "insufficient amount of water" is bound to receive the blame for this elasticity or toughness when it is not.
As a sausage maker gains experience, he will instinctively add just enough water to the mixture to form a meat "paste" with "peaks" remaining when the meat is pulled apart. Some have the experience to actually "hear" the load-bearing weight reduced from the motor of their processor as the correct amount of water is added at just the right point. My point is, be careful not to over-agitate the mixture. When peaks start to form in a "meat paste", get it into the stuffer.
Denaturation
Denaturation occurs when proteins are exposed to strong acids (vinegar) or bases, high concentrations of inorganic salts, or organic solvents such as alcohol. In addition, heat or even irradiation can cause denaturation. It also occurs when proteins are exposed to disruptive physical forces such as heat in cooking, or "kneading" a sausage mixture, or by the introduction of chemicals such as alcohol or vinegar in our home made sausages. A common example of a denatured protein is the albumin in an egg as it becomes hard-boiled with the introduction of heat. The gelatinous egg albumin becomes solid.
Proteins are large molecules composed of amino acids, which are arranged in a variety of complex structures. The "primary protein structure" is the simple linear sequence of amino acids within the protein. The "secondary protein structure" is divided into subgroups identified by three shapes. The "alpha helix" looks like a spiral staircase and is a structural protein. The "beta-pleated sheet" looks just like its name implies. The "random coil" does not have a specifically defined shape and this is the one found in collagen although it may link together alpha helices and beta sheets so that proteins may contain all three secondary structures.
Proteins also adopt a tertiary (third in order or formation) structure that is achieved by looping and folding the chain over itself. This folded structure occurs because certain portions of the molecules have an affinity for water. From here, the explanation gets overly scientific for us sausagemakin` wranglers. Suffice it to say, when a protein is denatured, the molecule's tertiary structure is corrupted, and this disruption affects the molecule's secondary (helical) structure without altering its primary structure. In other words, denaturation does not break any of the primary chemical bonds that link one amino acid to another but it changes the way the protein folds in upon itself. Again, denaturation occurs when proteins are exposed to strong acids or bases, high concentrations of inorganic salts, or organic solvents such as alcohol. In addition, heat or even irradiation can cause denaturation.
The process by which a protein structure assumes its functional shape is called "folding". This is the process by which polypeptides gain their functional three-dimensional structure called a "random coil" - effected by amino acids interacting with each other. Now, here`s the kicker! Whenever the three-dimensional structure of the protein is disrupted, the molecule's biological activity is affected and sometimes the effects may even be detrimental with side effects. Some denatured proteins can result in illness or even death.
In cattle, Bovine Spongiform Encephalopathy (Mad Cow) occurs when an infectious agent of a specific type of misfolded protein (called a "prion") is introduced. Indeed, several neurodegenerative diseases are believed to result from the accumulation of amyloid fibrills formed by these "misfolded" proteins. These prion proteins carry the disease between individuals and cause deterioration of the brain. In the case of BSE, the normal alpha helical - shaped protein molecules are distorted into a beta pleated sheet - the disease-causing shape of the particular protein.
However, not all denaturing processes are harmful. Certain denaturing processes are beneficial. Remember the "boiled egg"? And what about the sticky meat mass so vital to good texture in sausage? Without the development of actomyocin by the proteins actin and myocin, our sausage would literally fall apart.
So, the question remains. Does alcohol or an acid such as vinegar denature the proteins in meat? The answer is unquestionably yes. To see for yourself, try making a burger from meat that has had too much alcohol or too much vinegar added to it. It just won`t bind together. On the other hand, does it leave flavor behind. Again, yes it does. My favorite breakfast sausage is Italian Red Wine Sausage made with Spanish Sangria. What a flavor! Yes, somewhere there is a proper balance. This indeed is the solution to the question - HOW MUCH is appropriate? Somewhere there is a suitable tradeoff. There must be prudence and good judgment with the addition of alcohol or acidic compounds to our sausage.
One last thought on the matter. For some reason, when wine is slowly "sprayed" into meat being mixed to develop the actomyocin, it results in a much more tolerant acceptance. I can't explain it and I've never met anyone who can. There are many theories. All I know is that it works, providing not too much alcohol is added - in which case nothing will stop the proteins from unraveling.
May all you contractile myofibrillars remain in random coils!
Best Wishes,
Chuckwagon
You asked:
Okay, here are my thoughts - hope they help. (ummmm... remember - you asked)Regarding my marinating problem, avoiding using acid because it makes the sausage crumbly, what are your thoughts?
The body`s weight is about 15% proteins - large molecules made of hundreds of carbon, hydrogen, oxygen, and nitrogen atoms. Broken down into smaller parts, science identifies specific "amino acids". There are three types of meat proteins:
1. Sarcoplasmic (plasma) water soluble - myoglobin - belongs to this group (gives meat its color)
2. Myofibrillar (contractile) salt soluble - myosin and actin - belongs to this group (water-holding & emulsifying)
3. Stromal (connective) relatively insoluble - collagen and elastin - belong to this group (transmit movement)
Sarcopolasmic proteins are found in intracellular fluid and compose 30% of total muscle protein. They contribute only 20% to binding ability and the isoelectric point of its molecules is low, although they do contribute to tenderization through postmortem glycolysis, effecting a pH change. Sarcopalasmic proteins potentially add flavor contributions from a process known as "protein hydrolysis". Myoglobin consists of a typical amino acid protein concentration responsible for color intensity in meat. It was biologically designed to hold oxygen, and then release it for energy metabolism, so... it binds oxygen somewhat temporarily, dramatically changing meat`s color. Below are a few typical concentrations:
poultry white muscle .05 mg/g
chicken thigh 1.8-2.0 mg/g
turkey thigh 2.5-3.0 mg/g
pork, veal 1.0-3.0 mg/g
beef 4.0-10.0 mg/g
old beef 15.0-20.0 mg/g
mechanically separated meat 0.08-3.0 mg/g
Myofibrillar proteins are called the "contractile" proteins for the way they act upon muscle e.g. rigor mortis. Myofibrillar proteins are composed of 55% myosin - generally considered the single most important because of their long, highly-charged, "filament" molecule that is present in lean muscle. Actin and myosin are primarily responsible for creating the "sticky gel" that holds mixed, comminuted meat together.
Stromal proteins are in connective tissue and are primarily collagen, composing about 20 - 25% total body protein in the skin, sinews, tendons, etc. They are designed to transmit force to hold things together, thus they are generally tough and inert. Stromal proteins are of little or no value in processed meats as they have little binding ability. Further, as an animal ages, its meat becomes tougher due to the stromal protein`s unique make-up of 33% glycine and 10% hydroxyproline - responsible for non-charged or "non-polar" molecules having a minimally low isoelectric point. Stromal protein is generally considered a problem in processed meats and "high collagen meats" are often limited to 15 - 25% maximum, although chopped, ground, powdered collagen which can be dispersed, can be useful in forming a gel when heated. They may also be useful in retaining water and fat.
If sausage is overly mechanically-cut or tumbled, especially with the addition of salt or water, it may have the extraction of two of its myofibrillar proteins (myosin and actin) developed to a point where the structure of the final texture becomes more elastic than that in less-agitated processing. This elasticity may also be perceived as toughness or stiffness in texture. Most often an "insufficient amount of water" is bound to receive the blame for this elasticity or toughness when it is not.
As a sausage maker gains experience, he will instinctively add just enough water to the mixture to form a meat "paste" with "peaks" remaining when the meat is pulled apart. Some have the experience to actually "hear" the load-bearing weight reduced from the motor of their processor as the correct amount of water is added at just the right point. My point is, be careful not to over-agitate the mixture. When peaks start to form in a "meat paste", get it into the stuffer.
Denaturation
Denaturation occurs when proteins are exposed to strong acids (vinegar) or bases, high concentrations of inorganic salts, or organic solvents such as alcohol. In addition, heat or even irradiation can cause denaturation. It also occurs when proteins are exposed to disruptive physical forces such as heat in cooking, or "kneading" a sausage mixture, or by the introduction of chemicals such as alcohol or vinegar in our home made sausages. A common example of a denatured protein is the albumin in an egg as it becomes hard-boiled with the introduction of heat. The gelatinous egg albumin becomes solid.
Proteins are large molecules composed of amino acids, which are arranged in a variety of complex structures. The "primary protein structure" is the simple linear sequence of amino acids within the protein. The "secondary protein structure" is divided into subgroups identified by three shapes. The "alpha helix" looks like a spiral staircase and is a structural protein. The "beta-pleated sheet" looks just like its name implies. The "random coil" does not have a specifically defined shape and this is the one found in collagen although it may link together alpha helices and beta sheets so that proteins may contain all three secondary structures.
Proteins also adopt a tertiary (third in order or formation) structure that is achieved by looping and folding the chain over itself. This folded structure occurs because certain portions of the molecules have an affinity for water. From here, the explanation gets overly scientific for us sausagemakin` wranglers. Suffice it to say, when a protein is denatured, the molecule's tertiary structure is corrupted, and this disruption affects the molecule's secondary (helical) structure without altering its primary structure. In other words, denaturation does not break any of the primary chemical bonds that link one amino acid to another but it changes the way the protein folds in upon itself. Again, denaturation occurs when proteins are exposed to strong acids or bases, high concentrations of inorganic salts, or organic solvents such as alcohol. In addition, heat or even irradiation can cause denaturation.
The process by which a protein structure assumes its functional shape is called "folding". This is the process by which polypeptides gain their functional three-dimensional structure called a "random coil" - effected by amino acids interacting with each other. Now, here`s the kicker! Whenever the three-dimensional structure of the protein is disrupted, the molecule's biological activity is affected and sometimes the effects may even be detrimental with side effects. Some denatured proteins can result in illness or even death.
In cattle, Bovine Spongiform Encephalopathy (Mad Cow) occurs when an infectious agent of a specific type of misfolded protein (called a "prion") is introduced. Indeed, several neurodegenerative diseases are believed to result from the accumulation of amyloid fibrills formed by these "misfolded" proteins. These prion proteins carry the disease between individuals and cause deterioration of the brain. In the case of BSE, the normal alpha helical - shaped protein molecules are distorted into a beta pleated sheet - the disease-causing shape of the particular protein.
However, not all denaturing processes are harmful. Certain denaturing processes are beneficial. Remember the "boiled egg"? And what about the sticky meat mass so vital to good texture in sausage? Without the development of actomyocin by the proteins actin and myocin, our sausage would literally fall apart.
So, the question remains. Does alcohol or an acid such as vinegar denature the proteins in meat? The answer is unquestionably yes. To see for yourself, try making a burger from meat that has had too much alcohol or too much vinegar added to it. It just won`t bind together. On the other hand, does it leave flavor behind. Again, yes it does. My favorite breakfast sausage is Italian Red Wine Sausage made with Spanish Sangria. What a flavor! Yes, somewhere there is a proper balance. This indeed is the solution to the question - HOW MUCH is appropriate? Somewhere there is a suitable tradeoff. There must be prudence and good judgment with the addition of alcohol or acidic compounds to our sausage.
One last thought on the matter. For some reason, when wine is slowly "sprayed" into meat being mixed to develop the actomyocin, it results in a much more tolerant acceptance. I can't explain it and I've never met anyone who can. There are many theories. All I know is that it works, providing not too much alcohol is added - in which case nothing will stop the proteins from unraveling.
May all you contractile myofibrillars remain in random coils!
Best Wishes,
Chuckwagon
Last edited by Chuckwagon on Mon May 14, 2012 04:06, edited 2 times in total.
If it looks like a duck, walks like a duck, and quacks like a duck, it probably needs more time on the grill!
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Chuckwagon
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- Joined: Tue Apr 06, 2010 04:51
- Location: Rocky Mountains
I have eaten cantalope with white gravy and it is really very good. The cantalope is cold and the gravy is warm and served on different segments of the plate, wiping the 'lope through the puddle of gravy.
I have often wondered if since most of our tasting is olfactory do dogs and pigs have a finer sense of taste than people have.
I have often wondered if since most of our tasting is olfactory do dogs and pigs have a finer sense of taste than people have.
Ross- tightwad home cook
Chuckwagon wrote: "Some denatured proteins can result in illness or even death. An example would be denatured alcohol - a deadly poison to the human body." Actually, this form of denaturing refers to adding a poison to ethanol which renders it toxic, the additives being hard to separate. Our old buddies at Wikipedia have a writeup on it, if you're interested. http://en.wikipedia.org/wiki/Denatured_alcohol Nothing there about protein folding.
...although you might say that, when you have too much alcohol, your proteins fold. One way or the other, you fold.
Great writeup, though, Chuckwagon. I think I'll pour myself a glass of solvent (cabernet solvent-yawn, of course), and study it further. I guess the gist of the writeup is that if I spray a limited amount of my acidic marinade into the ground meat, then stuff, it'll hold together better? I'll give it a try. There's bound to be some way to get that flavor into the sausage.
Nice informative nugget on prions/BSE and protein folding. If more people understood this, we'd be more secure about red meat consumption. ...or else scared you-know-what-less.
...although you might say that, when you have too much alcohol, your proteins fold. One way or the other, you fold.
Great writeup, though, Chuckwagon. I think I'll pour myself a glass of solvent (cabernet solvent-yawn, of course), and study it further. I guess the gist of the writeup is that if I spray a limited amount of my acidic marinade into the ground meat, then stuff, it'll hold together better? I'll give it a try. There's bound to be some way to get that flavor into the sausage.
Nice informative nugget on prions/BSE and protein folding. If more people understood this, we'd be more secure about red meat consumption. ...or else scared you-know-what-less.
Experience - the ability to instantly recognize a mistake when you make it again.
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Chuckwagon
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- Joined: Tue Apr 06, 2010 04:51
- Location: Rocky Mountains
