Serine: Food Sources & Daily Intake

Table of Contents

1. How to Read These Tables
2. Recommended Intakes & Upper Limits
3. Bioavailability & Absorption
4. Cooking & Storage
5. Vegetarian & Vegan Sources
6. Who Needs to Pay Attention
7. Key Research Papers
8. Connections
9. Featured Videos

How to Read These Tables

• Non-essential amino acid. Your body can synthesize serine on its own — from glycine and from a glucose-breakdown intermediate — so a steady dietary supply is not required the way it is for the nine essential amino acids. Food still contributes, and serine comes along naturally with any protein you eat.
• Grams per 100 g, not %DV. There is no U.S. Food and Drug Administration Daily Value for individual amino acids, so this table reports the absolute grams per 100 g of food and ranks foods by that. A typical serving is shown beside each food.
• Complete vs incomplete protein. Animal foods are “complete” — they carry all the essential amino acids in good proportion and are serine-rich. Most single plant foods are lower in one or two essentials; eating a variety of legumes, nuts and seeds across the day covers the gaps.

Back to Table of Contents

Recommended Intakes & Upper Limits

Serine has no Daily Value: the U.S. food-label rules (21 CFR 101.9) set none for it, and the green and yellow marks in the food table above only rank each food against the richest food listed. The table below summarizes its status.

Back to Table of Contents

Bioavailability & Absorption

Serine from food is well absorbed as part of dietary protein, but it is one amino acid you rarely need to think about: the body manufactures its own from glycine and from a routine step in glucose metabolism, so internal supply — not the plate — sets how much you have. What food contributes is simply total protein quality and quantity: animal proteins (meat, poultry, fish, eggs, dairy) are complete and serine-dense, while plant proteins are a little lower and benefit from variety. Any normal protein intake supplies serine alongside everything else.

Back to Table of Contents

Cooking & Storage

Amino acids are stable to ordinary cooking — serine is not destroyed by normal heat, and cooking actually makes protein easier to digest. Very high, prolonged dry heat (charring) can damage some heat-sensitive amino acids, but typical cooking leaves serine intact.

Back to Table of Contents

Vegetarian & Vegan Sources

On a plant-based diet serine comes from two places: the body makes its own, and plant proteins supply it too. The strongest plant sources are lentils, white and other beans, chickpeas, peanuts, pumpkin and sunflower seeds, and walnuts. Eating a variety across the day (legumes + nuts + seeds) covers all the essential amino acids; serine itself is non-essential, so the body does not rely on a set amount of it from food.

Back to Table of Contents

Who Needs to Pay Attention

Dietary serine deficiency essentially never happens — the body synthesizes its own serine, so even diets low in it are covered. The best-known group who run short are people with rare inherited disorders of serine synthesis (such as 3-phosphoglycerate dehydrogenase deficiency and related serine-biosynthesis defects), where the body cannot make enough. Because the brain depends on locally made serine and the blood-brain barrier limits delivery from the bloodstream, these conditions affect the brain and nervous system — causing problems such as small head size (microcephaly), seizures and developmental delay — and are managed medically with serine (and sometimes glycine) supplementation, not through ordinary diet.

Low blood serine is not limited to those rare disorders. A 2023 review in the Annual Review of Nutrition describes low circulating serine in other genetic diseases and in chronic disease states, linked to damage in the nervous system, the retina (the light-sensing layer of the eye), the heart and ageing muscle. The same review notes that the brain makes its own serine locally, while the rest of the body gets most of its serine from glycine and one-carbon metabolism carried out in the liver and kidneys.

Two conditions show what low serine can do. In hereditary sensory and autonomic neuropathy type 1 (HSAN1), an inherited nerve disease, changes in the enzyme serine palmitoyltransferase raise the levels of toxic fats called deoxysphingolipids. In a 2019 randomized placebo-controlled trial, 18 adults with HSAN1 took high-dose oral L-serine (400 mg per kg of body weight a day) or a placebo for one year; 16 finished the study. The L-serine group’s neuropathy score (the Charcot-Marie-Tooth Neuropathy Score) improved compared with placebo (−1.5 points, p = 0.03), their deoxysphinganine level (one of the toxic fats) fell by 59% while it rose 11% with placebo, and no serious side effects were linked to L-serine.

A 2019 study in the New England Journal of Medicine tied the same toxic fats to an eye disease, macular telangiectasia type 2 (MacTel): of 11 people with HSAN1, 9 also had the eye disease. Among 125 people with MacTel who did not carry gene changes affecting serine palmitoyltransferase, deoxysphingolipid levels were 84.2% higher and serine levels 20.6% lower than in 94 unaffected people, and mice with lowered serine had more of these fats in the retina and poorer vision. A 2021 genetic study (Mendelian randomisation) concluded that genetically low serine is the primary metabolic driver of the disease and of how it progresses.

Back to Table of Contents

Key Research Papers

1. NIH MedlinePlus — Amino acids
2. National Academies — Dietary Reference Intakes: Protein and Amino Acids (2005), Chapter 10
3. PubMed — serine, glycine and one-carbon metabolism
4. PubMed — serine biosynthesis deficiency and the brain
5. Handzlik MK, Metallo CM. Sources and Sinks of Serine in Nutrition, Health, and Disease. Annual Review of Nutrition. 2023;43:123-151. — PubMed PMID: 37307855
6. Fridman V, Suriyanarayanan S, Novak P, David W, Macklin EA, McKenna-Yasek D, Walsh K, Aziz-Bose R, Oaklander AL, Brown R, Hornemann T, Eichler F. Randomized trial of l-serine in patients with hereditary sensory and autonomic neuropathy type 1. Neurology. 2019;92(4):e359-e370. — PubMed PMID: 30626650
7. Gantner ML, Eade K, Wallace M, Handzlik MK, Fallon R, Trombley J, Bonelli R, et al. Serine and Lipid Metabolism in Macular Disease and Peripheral Neuropathy. New England Journal of Medicine. 2019;381(15):1422-1433. — PubMed PMID: 31509666
8. Bonelli R, Ansell BRE, Lotta L, Scerri T, Clemons TE, Leung I, MacTel Consortium, Peto T, Bird AC, Sallo FB, Langenberg C, Bahlo M. Genetic disruption of serine biosynthesis is a key driver of macular telangiectasia type 2 aetiology and progression. Genome Medicine. 2021;13(1):39. — PubMed PMID: 33750426

Back to Table of Contents

Connections

• All Amino Acids
• Serine (Main Page)
• Serine Benefits
• Serine History
• Glycine
• Cysteine
• Threonine
• Eggs

Back to Table of Contents

Featured Videos

×