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The Most Important Amino Acid For Muscle Growth(and Fat Loss)
Most important amino acid for muscle growth (and fat loss)
When we start our fitness journey often, it’s motivated by wanting to lose weight and look better. If you’re like me, the only thing you knew is that you need to eat less if you're going to lose weight.
No one told me that if you’re just eating less, you’re going to lose more than body fat. You’ll lose muscle too. But that is the case.
You need to resistance train and eat a balanced diet, including protein, fats, and carbs. To protect your muscle mass while losing body fat. With protein playing a vital role.
We start with a very general understanding of nutrition, and over time we refine our knowledge, learning more detailed information as we go.
If you are interested in losing body fat and adding muscle, please email me at 1shark1bite@gmail.com for information on my personal training services.
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This brings us to our discussion today. We all know we need protein to repair and build new muscle. Amino acids are the building blocks of protein, and there is one amino acid that plays a more significant role than all the others. We must get enough in our food to maximally stimulate muscle protein synthesis.
Leucine is one of 3 branch chain amino acids that are known to stimulate muscle protein synthesis. These amino acids can’t be made in the body and must come from food.
The reason leucine is singled out, is it’s the most effective one at stimulating protein synthesis, which is the process of repairing and building new muscle tissue.
This doesn't just happen after our workouts. It's happening in our bodies all the time. It’s a continual process called protein turnover where older and damaged proteins in the cells are removed, called protein degradation and replaced with new proteins or protein synthesis.
If the removal of these damaged proteins happens faster than the rate of protein synthesis, then we have muscle wasting.
Another thing it does is enhance glucose and insulin homeostasis. Insulin and glucagon are hormones that work together to keep your blood sugar levels in check. When these hormones aren’t working properly, you’ll get food cravings, and you can even end up suffering from pre-diabetes and diabetes.
So how much leucine should we be taking every day? To try and find this, I read a wide range of recommendations, with the low end being about 14 milligrams per kg of bodyweight and the high end much as 45 mg.
The good news is if you are taking in enough protein from high-quality food sources, you’ll get all the Leucine you need.
Meats top the list of foods high in leucine, with chicken, beef, and pork leading the pack. Fish and dairy are also good sources.
Nowadays, many people are trying to cut back on their meat consumption. So for those navy beans are a great choice having slightly more leucine per 100g than milk. And tofu has even more.
Beans, in general, have a generous amount of leucine.
The next step down from beans is nuts and seeds. These contain about half or less of the amount of Leucine found in beans, but it’s still a reasonable amount. Pumpkin and squash seeds top this list, with hemp seeds following close behind.
Walnuts and pistachio’s head up the list for nuts.
Now I don’t want you to think I’m underestimating the importance of the other amino acids and, in particular, the 9 essential amino acids of which leucine is one of.
We need these amino acids to live, and our bodies can’t make them, so it’s critical we get them from food. This is why I always recommend whole food eating over taking supplements
If we just took a leucine supplement, we’d be neglecting the other essential amino acids that we need, along with all the vitamins and minerals necessary for optimal health.
First and foremost, we should always be looking at whole foods. To find out what mix of protein-based foods we should be eating to get maximum muscle growth, watch this video next and keep working out while having fun.
https://academic.oup.com/jn/article/133/1/261S/4687508
https://academic.oup.com/jn/article/136/1/256S/4664132
https://link.springer.com/article/10.2165/00007256-199927060-00001
https://academic.oup.com/jn/article/135/6/1553S/4663864
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