Walnuts vs Brazil Nuts – Which is Healthier?
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Our Verdict
When comparing walnuts to Brazil nuts, we picked the walnuts.
Why?
Talking macros first, they are about equal in protein, carbs, fats, and fiber; their composition is almost identical in this regard. However, looking a little more closely at the fats, Brazil nuts have more than 2x the saturated fat, while walnuts have nearly 2x the polyunsaturated fat. So, we’ll declare the macros category a moderate win for walnuts.
The category of vitamins is not balanced; walnuts have more of vitamins A, B2, B3, B5, B6, B9, C, and choline, while Brazil nuts have more of vitamins B1 and E. A clear and easy win for walnuts.
The category of minerals is interesting, because of one mineral in particular. First let’s mention: walnuts have more iron and manganese, while Brazil nuts have more calcium, copper, magnesium, phosphorus, potassium, and selenium. Taken at face value, this is a clear win for Brazil nuts. However…
About that selenium… Specifically, it’s more than 391x higher, and a cup of Brazil nuts would give nearly 10,000x the recommended daily amount of selenium. Now, selenium is an essential mineral (needed for thyroid hormone production, for example), and at the RDA it’s good for good health. Your hair will be luscious and shiny. However, go much above that, and selenium toxicity becomes a thing, you may get sick, and it can cause your (luscious and shiny) hair to fall out. For this reason, it’s recommended to eat no more than 3–4 Brazil nuts per day.
There is one last consideration, and this is oxalates; walnuts are moderately high in oxalates (>50mg/100g) while Brazil nuts are very high in oxalates (>500mg/100g). This won’t affect most people at all, but if you have pre-existing kidney problems (including a history of kidney stones), you might want to go easy on oxalate-containing foods.
For most people, however, walnuts are a very healthy choice, and outshine Brazil nuts in most ways.
Want to learn more?
You might like to read:
Why You Should Diversify Your Nuts
Take care!
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Glutathione: More Than An Antioxidant
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Glutathione’s Benefits: The Usual And The Unique
Glutathione is a powerful antioxidant that does all the things we might reasonably expect an antioxidant to do, plus some beneficial quirks of its own.
We do make glutathione in our bodies, but we can also get it from our diet, and of course, we can also supplement it.
What foods is it in?
It’s in a lot of foods, but some top examples include:
- turmeric
- avocado
- asparagus
- almonds
- cruciferous vegetables
- watermelon
- garlic
For a fuller list and discussion, see:
What does it do?
Let’s start with the obvious; as with most things that are antioxidant, it is also anti-inflammatory. Increasing or decreasing glutathione levels is associated with decreased or increased inflammation, respectively. For example:
It being anti-inflammatory also means it can be beneficial in calming autoimmune disorders:
Glutathione: a key player in autoimmunity
And to complete the triad of “those three things that generally go together”, yes, this means it also has anticancer potential, but watch out!
❝Although in healthy cells [glutathione] is crucial for the removal and detoxification of carcinogens, elevated [glutathione] levels in tumor cells are associated with tumor progression and increased resistance to chemotherapeutic drugs❞
~ Dr. Miroslava Cuperlovic-Culf et al.
Read in full: Role of Glutathione in Cancer: From Mechanisms to Therapies
So in other words, when it comes to cancer risk management, glutathione is a great preventative, but the opposite of a cure.
What were those “beneficial quirks of its own”?
They are mainly twofold, and the first is that it improves insulin sensitivity. There are many studies showing this, but here’s a recent one from earlier this year:
The Role of Glutathione and Its Precursors in Type 2 Diabetes
The other main “beneficial quirk of its own” is that it helps prevent and/or reverse non-alcoholic fatty liver disease, as in this study from last year:
Because of glutathione’s presence in nuts, fruits, and vegetables, this makes it a great thing to work in tandem with a dietary approach to preventing/reversing NAFLD, by the way:
Anything else?
It’s being investigated as a potential treatment for Parkinson’s disease symptoms, but the science is young for this one, so there is no definitive recommendation yet in this case. If you’re interested in that, though, do check out the current state of the science at:
Potential use of glutathione as a treatment for Parkinson’s disease
Is it safe?
While there is no 100% blanket statement of safety that can ever be made about anything (even water can kill people, and oxygen ultimately kills everyone that something else doesn’t get first), glutathione has one of the safest general safety profiles possible, with the exception we noted earlier (if you have cancer, it is probably better to skip this one unless an oncologist or similar advises you otherwise).
As ever, do speak with your doctor/pharmacist to be sure in any case, though!
Want to try some?
We don’t sell it, but here for your convenience is an example product on Amazon 😎
Enjoy!
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Blood, urine and other bodily fluids: how your leftover pathology samples can be used for medical research
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A doctor’s visit often ends with you leaving with a pathology request form in hand. The request form soon has you filling a sample pot, having blood drawn, or perhaps even a tissue biopsy taken.
After that, your sample goes to a clinical pathology lab to be analysed, in whichever manner the doctor requested. All this is done with the goal of getting to the bottom of the health issue you’re experiencing.
But after all the tests are done, what happens with the leftover sample? In most cases, leftover samples go in the waste bin, destined for incineration. Sometimes though, they may be used again for other purposes, including research.
Kaboompics.com/Pexels Who can use my leftover samples?
The samples we’re talking about here cover the range of samples clinical labs receive in the normal course of their testing work. These include blood and its various components (including plasma and serum), urine, faeces, joint and spinal fluids, swabs (such as from the nose or a wound), and tissue samples from biopsies, among others.
Clinical pathology labs often use leftover samples to practise or check their testing methods and help ensure test accuracy. This type of use is a vital part of the quality assurance processes labs need to perform, and is not considered research.
Leftover samples can also be used by researchers from a range of agencies such as universities, research institutes or private companies.
They may use leftover samples for research activities such as trying out new ideas or conducting small-scale studies (more on this later). Companies that develop new or improved medical diagnostic tests can also use leftover samples to assess the efficacy of their test, generating data needed for regulatory approval.
What about informed consent?
If you’ve ever participated in a medical research project such as a clinical trial, you may be familiar with the concept of informed consent. In this process, you have the opportunity to learn about the study and what your participation involves, before you decide whether or not to participate.
So you may be surprised to learn using leftover samples for research purposes without your consent is permitted in most parts of Australia, and elsewhere. However, it’s only allowed under certain conditions.
In Australia, the National Health and Medical Research Council (NHMRC) offers guidance around the use of leftover pathology samples.
One of the conditions for using leftover samples without consent for research is that they were received and retained by an accredited pathology service. This helps ensure the samples were collected safely and properly, for a legitimate clinical reason, and that no additional burdens or risk of harm to the person who provided the sample will be created with their further use.
Another condition is anonymity: the leftover samples must be deidentified, and not easily able to be reidentified. This means they can only be used in research if the identity of the donor is not needed.
Leftover pathology samples are sometimes used in medical research. hedgehog94/Shutterstock The decision to allow a particular research project to use leftover pathology samples is made by an independent human research ethics committee which includes consumers and independent experts. The committee evaluates the project and weighs up the risks and potential benefits before permitting an exemption to the need for informed consent.
Similar frameworks exist in the United States, the United Kingdom, India and elsewhere.
What research might be done on my leftover samples?
You might wonder how useful leftover samples are, particularly when they’re not linked to a person and their medical history. But these samples can still be a valuable resource, particularly for early-stage “discovery” research.
Research using leftover samples has helped our understanding of antibiotic resistance in a bacterium that causes stomach ulcers, Helicobacter pylori. It has helped us understand how malaria parasites, Plasmodium falciparum, damage red blood cells.
Leftover samples are also helping researchers identify better, less invasive ways to detect chronic diseases such as pulmonary fibrosis. And they’re allowing scientists to assess the prevalence of a variant in haemoglobin that can interfere with widely used diagnostic blood tests.
All of this can be done without your permission. The kinds of tests researchers do on leftover samples will not harm the person they were taken from in any way. However, using what would otherwise be discarded allows researchers to test a new method or treatment and avoid burdening people with providing fresh samples specifically for the research.
When considering questions of ethics, it could be argued not using these samples to derive maximum benefit is in fact unethical, because their potential is wasted. Using leftover samples also minimises the cost of preliminary studies, which are often funded by taxpayers.
The use of leftover pathology samples in research has been subject to some debate. Andrey_Popov/Shutterstock Inconsistencies in policy
Despite NHMRC guidance, certain states and territories have their own legislation and guidelines which differ in important ways. For instance, in New South Wales, only pathology services may use leftover specimens for certain types of internal work. In all other cases consent must be obtained.
Ethical standards and their application in research are not static, and they evolve over time. As medical research continues to advance, so too will the frameworks that govern the use of leftover samples. Nonetheless, developing a nationally consistent approach on this issue would be ideal.
Striking a balance between ensuring ethical integrity and fostering scientific discovery is essential. With ongoing dialogue and oversight, leftover pathology samples will continue to play a crucial role in driving innovation and advances in health care, while respecting the privacy and rights of individuals.
Christine Carson, Senior Research Fellow, School of Medicine, The University of Western Australia and Nikolajs Zeps, Professor, School of Public Health and Preventive Medicine, Monash University
This article is republished from The Conversation under a Creative Commons license. Read the original article.
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Ras El-Hanout
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This is a spice blend, and its name (رأس الحانوت) means “head of the shop”. It’s popular throughout Morocco, Algeria, and Tunisia, but can often be found elsewhere. The exact blend will vary a little from place to place and even from maker to maker, but the general idea is the same. The one we provide here today is very representative (and for an example of its use, see our Marrakesh Sorghum Salad recipe!).
Note: we’re giving all the quantities in whole tsp today, to make multiplying/dividing easier if you want to make more/less ras el-hanout.
You will need
- 6 tsp ground ginger
- 6 tsp ground coriander seeds
- 4 tsp ground turmeric
- 4 tsp ground sweet cinnamon
- 4 tsp ground cumin
- 2 tsp ground allspice ← not a spice mix! This is the name of a spice!
- 2 tsp ground cardamom
- 2 tsp ground anise
- 2 tsp ground black pepper
- 1 tsp ground cayenne pepper
- 1 tsp ground cloves
Note: you may notice that garlic and salt are conspicuous by their absence. The reason for this is that they are usually added separately per dish, if desired.
Method
1) Mix them thoroughly
That’s it! Enjoy!
Want to learn more?
For those interested in some of the science of what we have going on today:
- Our Top 5 Spices: How Much Is Enough For Benefits?
- A Tale Of Two Cinnamons ← this is important, to understand why it’s critical to use sweet cinnamon specifically
- Sweet Cinnamon vs Regular Cinnamon – Which is Healthier? ← not even exaggerating; one is health-giving and the other contains a compound that is toxic at 01.mg/kg; guess which one is easier to find in the US and Canada?
Take care!
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Successful Aging – by Dr. Daniel Levitin
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We all know about age-related cognitive decline. What if there’s a flipside, though?
Neuroscientist Dr. Daniel Levitin explores the changes that the brain undergoes with age, and notes that it’s not all downhill.
From cumulative improvements in the hippocampi to a dialling-down of the (often overfunctioning) amygdalae, there are benefits too.
The book examines the things that shape our brains from childhood into our eighties and beyond. Many milestones may be behind us, but neuroplasticity means there’s always time for rewiring. Yes, it also covers the “how”.
We learn also about the neurogenesis promoted by such simple acts as taking a different route and/or going somewhere new, and what other things improve the brain’s healthspan.
The writing style is very accessible “pop-science”, and is focused on being of practical use to the reader.
Bottom line: if you want to get the most out of your aging wizening brain, this book is a great how-to manual.
Click here to check out Successful Aging and level up your later years!
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It’s Not Fantastic To Be Plastic
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We Are Such Stuff As Bottles Are Made Of
We’ve written before about PFAS, often found in non-stick coatings and the like:
PFAS Exposure & Cancer: The Numbers Are High
Today we’re going to be talking about microplastics & nanoplastics!
What are microplastics and nanoplastics?
Firstly, they’renot just the now-banned plastic microbeads that have seen some use is toiletries (although those are classified as microplastics too).
Many are much smaller than that, and if they get smaller than a thousandth of a millimeter, then they get the additional classification of “nanoplastic”.
In other words: not something that can be filtered even if you were to use a single-micron filter. The microplastics would still get through, for example:
Scientists find about a quarter million invisible nanoplastic particles in a liter of bottled water
And unfortunately, that’s bad:
❝What’s disturbing is that small particles can appear in different organs and may cross membranes that they aren’t meant to cross, such as the blood-brain barrier❞
Note: they’re crossing the same blood-brain barrier that many of our nutrients and neurochemicals are too big to cross.
These microplastics are also being found in arterial plaque
What makes arterial plaque bad for the health is precisely its plasticity (the arterial walls themselves are elastic), so you most certainly do not want actual plastic being used as part of the cement that shouldn’t even be lining your arteries in the first place:
Microplastics found in artery plaque linked with higher risk of heart attack, stroke and death
❝In this study, patients with carotid artery plaque in which MNPs were detected had a higher risk of a composite of myocardial infarction, stroke, or death from any cause at 34 months of follow-up than those in whom MNPs were not detected❞
~ Dr. Raffaele Marfella et al.
(MNP = Micro/Nanoplastics)
Source: Microplastics and Nanoplastics in Atheromas and Cardiovascular Events
We don’t know how bad this is yet
There are various ways this might not be as bad as it looks (the results may not be repeated, the samples could have been compromised, etc), but also, perhaps cynically but nevertheless honestly, it could also be worse than we know yet—only more experiments being done will tell us which.
In the meantime, here’s a rundown of what we do and don’t know:
Study links microplastics with human health problems—but there’s still a lot we don’t know
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Protein: How Much Do We Need, Really?
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Mythbusting Protein!
Yesterday, we asked you for your policy on protein consumption. The distribution of responses was as follows:
- A marginal majority (about 55%) voted for “Protein is very important, but we can eat too much of it”
- A large minority (about 35%) voted for “We need lots of protein; the more, the better!”
- A handful (about 4%) voted for “We should go as light on protein as possible”
- A handful (6%) voted for “If we don’t eat protein, our body will create it from other foods”
So, what does the science say?
If we don’t eat protein, our body will create it from other foods: True or False?
Contingently True on an absurd technicality, but for all practical purposes False.
Our body requires 20 amino acids (the building blocks of protein), 9 of which it can’t synthesize and absolutely must get from food. Normally, we get those amino acids from protein in our diet, and we can also supplement them by buying amino acid supplements.
Specifically, we require (per kg of bodyweight) a daily average of:
- Histidine: 10 mg
- Isoleucine: 20 mg
- Leucine: 39 mg
- Lysine: 30 mg
- Methionine: 10.4 mg
- Phenylalanine*: 25 mg
- Threonine: 15 mg
- Tryptophan: 4 mg
- Valine: 26 mg
*combined with the non-essential amino acid tyrosine
Source: Protein and Amino Acid Requirements In Human Nutrition: WHO Technical Report
However, to get the requisite amino acid amounts, without consuming actual protein, would require gargantuan amounts of supplementation (bearing in mind bioavailability will never be 100%, so you’ll always need to take more than it seems), using supplements that will have been made by breaking down proteins anyway.
So unless you live in a laboratory and have access to endless amounts of all of the required amino acids (you can’t miss even one; you will die), and are willing to do that for the sake of proving a point, then you do really need to eat protein.
Your body cannot, for example, simply break down sugar and use it to make the protein you need.
On another technical note… Do bear in mind that many foods that we don’t necessarily think of as being sources of protein, are sources of protein.
Grains and grain products, for example, all contain protein; we just don’t think of them as that because their macronutritional profile is heavily weighted towards carbohydrates.
For that matter, even celery contains protein. How much, you may ask? Almost none! But if something has DNA, it has protein. Which means all plants and animals (at least in their unrefined forms).
So again, to even try to live without protein would very much require living in a laboratory.
We can eat too much protein: True or False?
True. First on an easy technicality; anything in excess is toxic. Even water, or oxygen. But also, in practical terms, there is such a thing as too much protein. The bar is quite high, though:
❝Based on short-term nitrogen balance studies, the Recommended Dietary Allowance of protein for a healthy adult with minimal physical activity is currently 0.8 g protein per kg bodyweight per day❞
❝To meet the functional needs such as promoting skeletal-muscle protein accretion and physical strength, dietary intake of 1.0, 1.3, and 1.6 g protein per kg bodyweight per day is recommended for individuals with minimal, moderate, and intense physical activity, respectively❞
❝Long-term consumption of protein at 2 g per kg bodyweight per day is safe for healthy adults, and the tolerable upper limit is 3.5 g per kg bodyweight per day for well-adapted subjects❞
❝Chronic high protein intake (>2 g per kg bodyweight per day for adults) may result in digestive, renal, and vascular abnormalities and should be avoided❞
Source: Dietary protein intake and human health
To put this into perspective, if you weigh about 160lbs (about 72kg), this would mean eating more than 144g protein per day, which grabbing a calculator means about 560g of lean beef, or 20oz, or 1¼lb.
If you’re eating quarter-pounder burgers though, that’s not usually so lean, so you’d need to eat more than nine quarter-pounder burgers per day to get too much protein.
High protein intake damages the kidneys: True or False?
True if you have kidney damage already; False if you are healthy. See for example:
- Effects of dietary protein restriction on the progression of advanced renal disease in the modification of diet in renal disease study
- A high protein diet has no harmful effects: a one-year crossover study in healthy male athletes
High protein intake increases cancer risk: True or False?
True or False depending on the source of the protein, so functionally false:
- Eating protein from red meat sources has been associated with higher risk for many cancers
- Eating protein from other sources has been associated with lower risk for many cancers
Source: Red Meat Consumption and Mortality Results From 2 Prospective Cohort Studies
High protein intake increase risk of heart disease: True or False?
True or False depending on the source of the protein, so, functionally false:
- Eating protein from red meat sources has been associated with higher risk of heart disease
- Eating protein from other sources has been associated with lower risk of heart disease
Source: Major Dietary Protein Sources and Risk of Coronary Heart Disease in Women
In summary…
Getting a good amount of good quality protein is important to health.
One can get too much, but one would have to go to extremes to do so.
The source of protein matters:
- Red meat is associated with many health risks, but that’s not necessarily the protein’s fault.
- Getting plenty of protein from (ideally: unprocessed) sources such as poultry, fish, and/or plants, is critical to good health.
- Consuming “whole proteins” (that contain all 9 amino acids that we can’t synthesize) are best.
Learn more: Complete proteins vs. incomplete proteins (explanation and examples)
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