MSG: The devil in disguise or disguised as the devil?

Over the past 24 hours on my facebook feed, I have seen two posts on MSG, and so I figured this is as good a time as any to help debunk the myth of ‘evil MSG’. So… here is the suspect: Monosodium glutamate.
631px-Monosodium_glutamate

I’m not really that bad… or am I?

You may have heard that MSG is not good for you. You may also have heard that it is present in asian foods (I know that I have seen signs on a number of local take-away joints stating ‘We do not use MSG’). So, with a nice little abbreviation, or in its chemical name, it is easy to spread the word that it is an evil chemical which is bad for you. But, with a little extra chemistry knowledge, a look at the history of research into MSG, and the understanding that just because it has a chemical name doesn’t mean that it will kill you (see ‘sodium chloride’- AKA table salt), you can start to see that this ‘evil’ label is not deserved.

So, lets start with that chemistry knowledge. Monosodium glutamate is a sodium salt (where sodium is that ‘Na’ in the diagram above). In chemistry, what we find with salts is that because they have those little positive and negative signs (charges), they are easier to dissolve in water than things without those charges. They also form crystals much more easily (see sodium chloride once again, those nice crystallised pieces of table salt!)

Sodium_chloride_wiki

Mmmm, delicious salt. 

That’s all well and good, but what does that have to do with anything? Well, to give you a little more chemistry knowledge, I’d like to show you another chemical structure. This time, it’s glutamic acid.

Glutamic_acid

Glutamic acid.

Wait a minute, that looks just like… ? Before we go any further, let’s talk about glutamic acid. Glutamic acid is an amino acid, which means that it is a part of many of the foods that we consume each day. Why? Because amino acids make up protein. Protein is present in many foods and beverages, including meats, milk, eggs, nuts, and legumes. The funny thing about glutamic acid is that it is considered non-essential in the human diet; in other words, it is’t necessary for us to eat proteins with lots of glutamic acid BECAUSE WE MAKE IT IN OUR BODIES ANYWAY.

So I could go into detail about how MSG got the bad rap it appears with today, but I think that the American Chemical Society have done a much better job: Check out the Video “Is MSG Bad for You?“, which was created by the ACS (You can follow their Facebook page on Everyday Reactions here). The take-home message from the video is one of the very things I am trying to prove in my blog: If someone tells you that something is bad for you but you can’t find a definitive answer as to why, then it is YOUR job to dig in and research.

While you’re out watching and learning, there’s also this fantastic infographic by Compound Interest: You can view the infographic below, or click on this link for a larger version.

MSG infographic

 

The Undeserved Reputation of MSG.

Enjoy, and feel free to comment with your thoughts, or any questions you have which I can address in future posts 🙂

http://www.berries.com/blog/science-of-baking

The Science of Baking

Check out this awesome infographic describing the chemical nature of baking

http://www.berries.com/blog/science-of-baking

Mmmmm… cake….

I have heard a number of times the similarities between cooking/ baking and science in a lab. Throw together a few ingredients, stir them, heat them (I’ve even used a scientific form of ‘microwave’), and voila! Delicious products. Although you probably shouldn’t eat the laboratory ones. Unless you really, really, REALLY want superpowers and aren’t afraid to die in your attempt.

Don’t we all…

The similarities don’t end there. Heat it for too short a period, chances are you’ll end up with a gooey mess (assuming that’s not what you wanted). Heat it for too long or set the temperature too high, blackened mess. Use out of date or impure starting materials, forget to add something, and you also miss out on synthesising your desired product.

This infographic (originally posted on Shari’s Berries) shows just that, and it brings together many of the elements of the food science unit I teach to first years: Proteins (in eggs, milk, and flour), fats (in milk, butter and oils), and carbohydrates (in flour and sugars), as well as yeast, baking soda, and water. All of these ingredients come together to perform separate roles. For example, one role of the fats and oils in baking is to repel water (have you ever noticed how oil and water don’t mix? Here’s why: Polar and Non-Polar Compounds – ignore the ‘practical’ explanation). So by repelling water, water is no longer able to interact with certain proteins, in particular gliadin and glutenin, which together with water make gluten (I’ll be posting soon about gluten). If lots of gluten forms quickly, you end up with a dough that doesn’t rise well. So by using fats to repel water, there is a slow and steady production of gluten, which leads to a nicely formed dough which will rise well. 

http://www.berries.com/blog/science-of-baking

Side note: Gluten is not the enemy (unless you have coeliac disease).

Another example of the chemical interaction of a baking ingredient is baking soda. Baking soda is known as sodium bicarbonate, and is a ‘leavening agent’. This means that when it reacts with acids in the baking mixture, it releases carbon dioxide. It is this carbon dioxide that helps to form bubbles in the dough, helping it to rise. 

http://lolwtfcomics.blogspot.com.au/2012/01/love-is-in-air-false-nitrogen-oxygen.html

It’s okay, carbon dioxide in your bread won’t kill you. 

So the next time you’re planning on baking a cake, think about why you add so many different ingredients for a perfect, delicious product.

And then bring me some cake. I love cake.

More Retronasal Bonito, Monsieur?

Generally, if people decide that a food is too bland at the dinner table, they add salt. However, more and more people are being made aware of the problems that salt (in particular, sodium) can cause to the body: high blood pressure, kidney problems, and even stroke. So what do we do?

Add dried bonito stock, according to Japanese researchers.

Bonito is a type of fish, and dried bonito stock and flakes are commonly used in Japanese cooking, especially soups. They are associated with umami flavour.

Bonito Stock

Bonitooooooooooo.. Used in miso soup!

The interesting part here is how we as humans are able to perceive the smell of bonito. It doesn’t come through sniffing food through our nose (known as the orthonasal pathway). Instead, we perceive the aroma of bonito through the retronasal pathway- that is, after we chew (and even swallow) our food, the aroma is released and travels from our mouth into our nasal cavity.    

Retronasal Bonito

A photo of the setup used to provide retronasal bonito aroma (taken from the article).

Using two forms of bonito stock (arabushi and karebushi), the researchers tested if retronasal bonito enhanced the saltiness of foods (which it didn’t) and also if it increased the palatability of food (which it did).

While this is all well and good, one thing that the researchers note is that bonito, while delicious and flavoursome and enjoyed by many Japanese, is not as appreciated in other cultures. Therefore, bonito may not be the answer to everyone’s low-salt-tasteless-diet woes.  

The Article: Retronasal Odor of Dried Bonito Stock Induces Umami Taste and Improves the Palatability of Saltiness

The Authors: Mariko Manabe, Sanae Ishizaki, Umi Yamagishi, Tatsuhito Yoshioka and Nozomu Oginome

The Journal: Journal of Food Chemistry, 2014

All About Lab Safety…

So, here’s a picture of me and my lab mate:

ShoeSafetyJump

Jumping for joy! That’s me on the right 🙂

Why are we so happy, you ask? We had just finished filming (and photographing) a video based on the correct footwear to wear in a lab. 

I’m a University lecturer, and I love teaching in the lab. It’s probably my favourite part of the job. You can see from the photo above that our School recently got some brand-spanking-new food science laboratories. They’re beautiful and bright and clean. Yet, to be honest, they’re not entirely safe. 

Don’t get me wrong. They weren’t built incorrectly. They don’t have extremely sharp corners for people to bump into. They don’t have people hiding in dark corners, ready to prey on unsuspecting students with handfuls of candy.

But they’re not entirely safe.

Any science lab is not entirely safe.

That’s why every (good) lab that you walk into has a set of strict rules. Some of these rules include that you must tie your hair back, and wear a lab coat, gloves, and safety glasses. Why? Because we’re not dealing with salt and sugar and vinegar, like in your kitchen at home. Some of the solutions and reagents that are used within these laboratories may burn through your clothes. Others may (most likely won’t and definitely shouldn’t, but may) spontaneously burst into flame if a room gets too warm. If you drop some of these solutions on a bench and splash up into your eye, well… you may never see again. So you are asked to protect yourself.

The same applies to shoes. If you walk into a lab wearing sandals, or thongs, or ugg boots, and you drop a strong acid solution on your feet, you are going to know about it. In our lab, if you don’t wear the correct and safe footwear, you are asked to wear the ‘gumboots of shame’. Yup, they’re just as embarrassing as you imagine.

So now I’m sure you understand why we’re so excited about safe footwear in the lab… Because we don’t have to wear the gumboots of shame 😉

Not-So-Nuts about Nuts?

If you have a nut allergy, what’s the first thing you do when someone offers you a handful… Politely say no and hold your breath as you walk away? Scream and run? Or cower in a corner, rocking back and forth?

When a person who is allergic to nuts comes into contact with one, what happens is that the body recognises particular proteins from the nuts. The body then produces antibodies called “Immunoglobulin E” (IgE), which binds to these proteins. Once the IgE and protein are bound together, the body turns on all alerts – cue flashing red lights and sirens – and responds by causing anything from mild itching to anaphylaxis (the closing of the airways).

So if your response to an offering of nuts was any of the above, I wouldn’t blame you. At the moment, the main way to prevent any allergic reactions is to avoid nuts altogether.

What if the nut-wielding fiend told you that you wouldn’t have an allergic reaction to this particular handful? Sound too good to be true?

Researchers in America are currently investigating ways in which they can change the chemical structure of the proteins in cashews that are responsible for allergic reactions. As the protein structure is not the same, IgE finds it more difficult to identify these proteins. If the IgE doesn’t bind the protein, no alerts and no allergic response.

There are a few different ways in which to alter the structure of proteins, however many of these ways involve harsh chemicals. Chris Mattison, PhD, who leads the teams researching the de-allergenisation (I may have made that word up) of cashews, says that they were aiming for a way to change the protein structure using much safer reagents, and found that the generally regarded as safe (GRAS) sodium sulphite worked a treat. The aim is to eventually apply this same technique to other nuts, including peanuts.

Where I found this story: Making cashews safer for those with allergies

More information on Mattison’s Research Project: Primary and Secondary Prevention of Peanut and Tree Nut Allergy

Time to start posting!

So, after a very lengthy break, I’M BACK! I wanted to start off with something that will hopefully become a common theme on my blog, and that is reviews of articles related to food science, food analysis and sensory evaluation of food… So here you go!

It’s Quick-Journal-Article-Review-Time! Or QJART as it shall now be known. This QJART is based on the following article:

     Effect of vine foliar treatments on the varietal aroma of Monastrell wines

     A.I. Pardo-García, K. Serrano de la Hoz, A. Zalacain, G.L. Alonso & M.R. Salinas.

     Food Chemistry 163 (2014) 258-266

It turns out winemakers can induce grapes to smell like smoke/ clove or whisky.

This area of research began after it was noted that grapes from areas which had experienced forest fire activity were producing wines with a smokey flavour. It was realised that the foliar treatment of certain volatile/ aroma compounds (such as those present in smoke) to grape vines was allowing the storage of these compounds as non-volatile glycosides (basically, by joining the volatile to a sugar molecule). Then, during the wine-making process, the volatiles could be released to provide their associated smell.

The analysis involved the use of Gas Chromatography- Mass Spectrometry (GC-MS) to identify the aroma/ volatile compounds in the grapes/ wine, as well as analysis of the amount of glycosidic compounds by High Performance Liquid Chromatography (HPLC), and sensory analysis by a team of eight expert judges. These analyses were completed at three stages of the winemaking process: at the end of the alcoholic fermentation, and malolactic fermentation (the addition of bacteria), as well as six months later.

Using eugenol and guaiacol (smoke aroma compounds), and whiskey lactones (you guessed it, they make up the aroma of whiskey) in Monastrell red grapes, researchers in Spain identified an increase in glycoside content in grapes, but noted that there was little transferrance to wines, suggesting that these glycosides are stored in the grape’s skins. Also, the storage of guiaiacol in grapes was associated with lower sugar content (leading to lower alcohol levels in wine).

Even though the transferrance of aroma compounds to wines was quite small (an increase of 8-12% at most), tasters were still able to identify clove (eugenol and guaiacol) and woody/oak (whiskey lactone) flavours.

No word on when we will be receiving the first batch of ‘bacon’ wine.