Mind and Body Connection

Mind and Body Connection James Maloney's Mind and Body Connection

James is a qualified Naturopath and acupuncturist who has received honours in Psycho-therapy and Counselling and specializes in herbal medicine solutions and nutritional health, with over 16 years of clinical experience and outstanding results in all areas.

James Maloney
06/06/2026

James Maloney

Eat breakfast before lunch, and your blood sugar may rise only slightly.

Skip breakfast, eat the exact same lunch, and that rise may be much higher.

The interesting part is that the food did not change. The timing did.

A small study in healthy adults looked at this by giving people the same lunch on two different days. On one day, they ate breakfast first. On the other, they skipped breakfast. After the skipped-breakfast lunch, their blood glucose rose much more: about 3.2 mmol/L compared with 0.9 mmol/L on average.

Same people. Same lunch. Different morning.

This does not mean breakfast is automatically “good” or skipping breakfast is automatically “bad.” The study was small, so it is better seen as a useful clue rather than a fixed rule. But it does show something important: the body’s response to a meal depends on the state it is in before that meal arrives.

One possible explanation is free fatty acids. When you go without food for several hours, fatty acids can rise in the blood. If muscle is running more on fat, it may take up less glucose when lunch arrives. So more of that glucose can stay in circulation for longer.

When breakfast is eaten, those fatty acids may stay lower, which could leave the muscles more ready to absorb the glucose from the next meal.

There is also a separate study in people with type 2 diabetes where arginine before lunch reduced the post-lunch glucose rise by about half. Arginine is an amino acid, not a carbohydrate meal, so this again points to the idea that what happens before a meal can change how the body handles that meal.

The honest limitation is that these are small, short-term studies. They measured what happened over a single afternoon, not what happens over months or years. The wider research on breakfast is mixed, and this should not be turned into a hard diet rule.

But it does suggest this:

Your glucose response is not only about the meal. It is also about the condition your body is in when the meal arrives.

So the same lunch may behave differently depending on whether your body is calm, fed, stressed, fasted, under-slept, or already running on stored fuel.

Food matters. But context matters too.

References:
Jovanovic et al., Clinical Science, 2009
Jovanovic et al., Diabetes Care, 2009
Wolever et al., American Journal of Clinical Nutrition, 1988

Eat breakfast before lunch, and your blood sugar may rise only slightly.Skip breakfast, eat the exact same lunch, and th...
06/06/2026

Eat breakfast before lunch, and your blood sugar may rise only slightly.

Skip breakfast, eat the exact same lunch, and that rise may be much higher.

The interesting part is that the food did not change. The timing did.

A small study in healthy adults looked at this by giving people the same lunch on two different days. On one day, they ate breakfast first. On the other, they skipped breakfast. After the skipped-breakfast lunch, their blood glucose rose much more: about 3.2 mmol/L compared with 0.9 mmol/L on average.

Same people. Same lunch. Different morning.

This does not mean breakfast is automatically “good” or skipping breakfast is automatically “bad.” The study was small, so it is better seen as a useful clue rather than a fixed rule. But it does show something important: the body’s response to a meal depends on the state it is in before that meal arrives.

One possible explanation is free fatty acids. When you go without food for several hours, fatty acids can rise in the blood. If muscle is running more on fat, it may take up less glucose when lunch arrives. So more of that glucose can stay in circulation for longer.

When breakfast is eaten, those fatty acids may stay lower, which could leave the muscles more ready to absorb the glucose from the next meal.

There is also a separate study in people with type 2 diabetes where arginine before lunch reduced the post-lunch glucose rise by about half. Arginine is an amino acid, not a carbohydrate meal, so this again points to the idea that what happens before a meal can change how the body handles that meal.

The honest limitation is that these are small, short-term studies. They measured what happened over a single afternoon, not what happens over months or years. The wider research on breakfast is mixed, and this should not be turned into a hard diet rule.

But it does suggest this:

Your glucose response is not only about the meal. It is also about the condition your body is in when the meal arrives.

So the same lunch may behave differently depending on whether your body is calm, fed, stressed, fasted, under-slept, or already running on stored fuel.

Food matters. But context matters too.

References:
Jovanovic et al., Clinical Science, 2009
Jovanovic et al., Diabetes Care, 2009
Wolever et al., American Journal of Clinical Nutrition, 1988

Your body can only use 25-30 grams of protein per meal. Anything above that gets wasted." This is one of the most widely...
16/04/2026

Your body can only use 25-30 grams of protein per meal. Anything above that gets wasted." This is one of the most widely repeated claims in fitness nutrition. It has been repeated for over a decade, and it was always based on incomplete data. Not wrong data. Incomplete data. The studies that built this claim were measuring the right thing over the wrong timescale.The origin of the claim traces to dose-response studies in the late 2000s. Moore et al. (2009, Am J Clin Nutr) gave young men 0, 5, 10, 20, or 40g of egg protein after leg-only resistance exercise and measured muscle protein synthesis for approximately 4 hours. They found that MPS plateaued at 20g with no further increase at 40g, and that amino acid oxidation increased at the higher dose. This was a well-designed study, but it had three important limitations: only 6 subjects, only leg exercise, and only a 4-hour window. Witard et al. (2014, Am J Physiol) repeated a similar design with whey protein at 0, 10, 20, and 40g. They found a trend toward higher MPS at 40g compared to 20g, but the difference did not reach statistical significance, likely because the study had only 12 subjects per group and a similarly short measurement period. These two studies became the foundation for the 20-25g recommendation. Fitness culture rounded it to 30g. The number calcified.But there were early cracks. Macnaughton et al. (2016, Physiol Rep) tested 20g versus 40g of whey protein after whole-body resistance exercise rather than leg-only exercise. With 30 resistance-trained men divided into higher and lower lean body mass groups, they found that 40g produced significantly greater MPS than 20g regardless of body size. Their explanation: whole-body exercise activates more muscle tissue, disperses blood flow more broadly, and therefore requires more amino acids to reach each muscle group. This was the first published evidence that the "ceiling" might depend on how much muscle you just trained, not a fixed biological limit.Trommelen et al. (2023, Cell Reports Medicine) settled it. They gave 36 recreationally active young men either 0g, 25g, or 100g of milk protein after a 60-minute whole-body resistance exercise session and tracked muscle protein synthesis for 12 hours using a quadruple isotope tracer approach.Here is why this matters. Think of your digestive system like a funnel. The funnel has a fixed flow rate. If you pour a cup of water through it, it drains in minutes. If you pour a gallon in, the funnel does not overflow. The water sits above the opening and drains at the same rate over a longer period. Protein works the same way. A 25g dose digests quickly, amino acids peak in the blood within a couple of hours, MPS peaks shortly after, and by about 6 hours the process is done. A 100g dose does not overwhelm the system. The stomach slows gastric emptying. The intestine releases amino acids gradually over many hours. Each wave of amino acids that arrives finds muscle tissue ready to incorporate them. The body does not waste the protein. It just takes longer to process it.This is exactly what Trommelen found. The 25g dose elevated MPS for approximately 6 hours, then returned to baseline. The 100g dose was still elevated at 12 hours when the study ended. The advantage of the larger dose was modest in the first 4 hours but became substantially larger from hours 4 through 12. That is the window every previous study missed.The oxidation question is the other half of the ceiling argument. The claim was that protein above 20-25g just gets burned for energy. Trommelen measured this directly: in the first 4 hours, less than 15% of ingested protein-derived amino acids from the 100g dose were oxidized. The vast majority were incorporated into tissue protein, including muscle, connective tissue, and plasma proteins. The paper states it plainly: "Protein ingestion has a negligible impact on whole-body protein breakdown rates or amino acid oxidation rates."Caveats matter here. This study was conducted in recreationally active young men, not trained athletes, not women, not older adults. A 2024 commentary by Witard and Mettler in the International Journal of Sport Nutrition and Exercise Metabolism specifically cautioned that this finding may not translate to resistance-trained young women. Older adults with blunted anabolic sensitivity might also respond differently. Nobody has repeated this protocol in those populations with a 12-hour window yet.This was also an acute MPS study, not a longitudinal hypertrophy trial. More muscle protein synthesis over 12 hours does not automatically mean proportionally more muscle over 12 weeks. MPS is a building rate measured at one time point. It correlates with long-term outcomes but is not a guarantee.One disclosure: a co-author was employed by FrieslandCampina, a dairy company. The company had no role in funding, data collection, analysis, or manuscript preparation per the conflict of interest statement. The Macnaughton 2016 study was funded by GlaxoSmithKline. Industry involvement in protein research is common. It does not invalidate findings, but it is part of a complete read.The study used milk protein as a liquid, not a steak dinner. A mixed meal with fat, fiber, and other macronutrients would slow gastric emptying further, likely extending the absorption window even more. Real-world meals may show an even more prolonged response than this controlled protocol captured.What this means practically: you do not need to eat exactly 25-30g of protein every 3 hours to avoid "wasting" it. If you eat a larger meal, your body will use the protein. It will just take longer to digest and absorb, and the anabolic window extends accordingly. Distribution across the day still has value for satiety, blood sugar, and hitting your daily target. But the biological case for rigid per-meal portioning is weaker than the fitness industry claimed for two decades. The ceiling was never in the muscle. It was in the clock.Moore et al., Am J Clin Nutr, 2009Witard et al., Am J Physiol, 2014Macnaughton et al., Physiol Rep, 2016Trommelen et al., Cell Rep Med, 2023

Methylation is one of the most discussed topics in functional health. Most of the conversation centers on folate and B12...
09/04/2026

Methylation is one of the most discussed topics in functional health. Most of the conversation centers on folate and B12. The actual cycle has four nutrient inputs, and the one almost nobody is getting enough of is rarely mentioned.The methylation cycle converts homocysteine back to methionine, which gets activated to SAM, your body's universal methyl donor. SAM donates methyl groups to DNA, neurotransmitters, phospholipids, creatine, and hundreds of other reactions. Once it donates, it becomes SAH, then homocysteine, and the cycle has to turn again.Two nutrients drive the main recycling step. Folate (as 5-MTHF) provides the methyl group. B12 (as methylcobalamin) is the cofactor methionine synthase needs to transfer it. These are the two everyone focuses on. Post-fortification, only about 12% of US adults fall below the EAR for folate, and 5% for B12. These are relatively well covered in the food supply.B6 runs the exit valve. When homocysteine accumulates faster than it can be recycled, cystathionine beta-synthase (CBS) shunts the excess into the transsulfuration pathway, producing cysteine and eventually glutathione. Without adequate B6, that exit is restricted. Homocysteine backs up even if folate and B12 are sufficient.Then there is choline. Your liver converts choline to betaine, which feeds BHMT, a backup remethylation enzyme that works completely independently of folate and B12. This pathway is especially active in the liver and kidney. NHANES data shows 92% of US adults fall below the adequate intake for choline. It is the single most prevalent nutrient gap in this entire cycle, and it is almost never included in methylation protocols.What this means practically: if you are addressing methylation, checking folate and B12 status is a starting point, not the full picture. B6 status matters independently because it controls the exit, not just the recycling. And choline intake deserves attention proportional to the gap: eggs are the most concentrated whole food source (one large egg provides roughly 150 mg against a 550 mg AI for men, 425 mg for women). Betaine from beets and spinach also feeds BHMT directly.The pattern worth noticing: the nutrient with the highest inadequacy in this cycle is the one least likely to appear in a methylation product.Reider et al., Nutrients, 2020.Wallace & Fulgoni, Nutrients, 2017.

26/03/2026

When a client comes to me to work on their anxiety, depression, ADHD, mood swings and literally any mental health picture- I show them this chart. It's simple: we can't produce the happy neurotransmitters (serotonin) and the motivation neurotransmitters (dopamine) without eating enough protein and digesting that protein. Without strong levels of Hcl - hydrochloric or stomach acid we cannot properly break down the protein into individual amino acids to make serotonin and dopamine. In addition, many people are deficient in B vitamins, magnesium, zinc and other co-factors needed to keep the pathways in the chart going. Did you know that serotonin converts to melatonin? So if you have sleep issues you can now also see why. I use this chart often in clinic to help clients understand why they have mood issues and low motivation. If you are vegan, this situation is made 1000 times worse. Chart credit- Dr Igor Tabrizian, "The Visual Textbook of Nutritional medicine".

Traditionally, herbalists have used elecampane to treat coughs, particularly those associated with bronchitis, asthma, a...
06/11/2025

Traditionally, herbalists have used elecampane to treat coughs, particularly those associated with bronchitis, asthma, and whooping cough.

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Elderflower benefits include traditional uses for respiratory issues like colds, flu, and sinus infections, as well as a...
04/11/2025

Elderflower benefits include traditional uses for respiratory issues like colds, flu, and sinus infections, as well as antioxidant, anti-inflammatory, and skin-calming properties. It contains antioxidants and bioflavonoids that can help protect cells from damage.

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This in an amazing herb, it helps with relief of upper respiratory tract infections, including mild tonsillitis, pharyng...
03/11/2025

This in an amazing herb, it helps with relief of upper respiratory tract infections, including mild tonsillitis, pharyngitis, cold and flu. Relief of mild bronchitis. To support the body's resistance to infections of all kinds. Skin complaints, boils. Internally and topically to support healthy wound healing. Internally and topically for mild mouth ulcers. Topically as a gargle to relieve mild tonsillitis. Topically as a mouthwash to support healthy gums.

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www.mindandbodyconnection.com.au

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