Tejas Kulkarni Profile picture
Feb 28 7 tweets 4 min read Read on X
Cooked rice should not be left out for more than a few hours.

Consume it within few hours or If not consuming it within 4-6 hours then store it in the fridge at 4 °C or below (after cooling slightly) to prevent the growth of toxic spore-forming bacteria.

You might ask is this Cereus? 😬
Yes.

Bacillus cereus, a spore-forming bacterium naturally present in uncooked rice can be the problem

bacteria can multiply rapidly , almost doubling every 20 minutes. This exponential growth means bacterial counts can reach dangerous levels after few hours.
According to one study,
Cooking didn’t kill all spores. Boiling rice ~15 min left some Bacillus cereus spores alive; 4/8 strains survived cooking.

Temperature after cooking matters a lot

30 °C (warm kitchen): several strains started growing within 12 h and reached ~10^5 CFU/g by 18–24 h. Reported generation times were ~1.2 h at 30 °C (fast doubling).

25 °C (room temp): growth appeared by 24–48 h depending on strain.

4 °C (fridge): no detectable growth for 7 days (for this organism, in this model).

pmc.ncbi.nlm.nih.gov/articles/PMC99…
Under ideal growth conditions (moist, starchy food at ~30 °C / 86 °F):

B. cereus can reach toxin-producing levels (≥10⁵–10⁷ CFU/g) in as little as 4–6 hours.

Significant toxin accumulation can occur within 8–12 hours at room temperature.

Things to consider:
Emetic toxin (Cereulide) - Heat-stable, survives cooking/reheating, causes nausea/vomiting in 1–6 h,

Enterotoxins – Heat-labile, destroyed by reheating, cause diarrhea/cramps in 6–15 h.

Once cereulide forms, no cooking can destroy it ,prevention is the only protection.
Prevention of cereulide
1. Cool quickly – ≤21 °C in 2 h (1 h if hot weather), shallow containers, stir occasionally.
2.Refrigerate promptly – ≤4 °C in airtight containers, never keep “warm” overnight.
3.Limit storage – Fridge 3–4 days, freezer 3 months.
4.Reheat safely – ≥74 °C, once only, eat immediately.
5.Avoid high-risk – Buffet/lukewarm rice, uncooled transport, rice >2 h at room temp, sour/slimy rice.
Safety while reheating-

Always reheat rice to 165°F (74°C) throughout before consumption.

Reheating Methods
Microwave: Add 1-2 tablespoons of water per cup, cover, and heat until steaming hot

Stovetop: Add liquid, cover, and heat thoroughly while stirring

Oven: Cover and heat until internal temperature reaches 165°F

Important:

Only reheat the portion you plan to consume immediately

Never reheat rice more than once - repeated heating increases contamination risk

Do not leave reheated rice at room temperature after heating
Many of us, including at our home we have curd rice -
When you add curd (dahi) to cooked rice, you change the food environment in two main scientific ways:
(1) the pH drops because lactic acid makes the mixture more acidic, which can slow the growth of many bacteria
(2) you introduce live lactic-acid bacteria that will keep fermenting the sugars and make the rice more sour over time, especially if it’s kept warm.

But this does not “sanitize” the rice,cooked rice can contain heat-resistant spores of Bacillus cereus that survive cooking, and if rice has already sat warm for long enough, bacteria may have multiplied or produced toxins adding curd later doesn’t reverse that.

So whether you add curd or not, the safest rule is still time + temperature control, cool rice quickly, then store it in the refrigerator at ~4°C in a clean, closed container to strongly slow bacterial growth, and it can usually be consumed the next day with a much lower risk.
Practical points:
This doesn’t mean “don’t eat rice the next day.”
It means rice is totally fine next day if you store it properly.
The risk comes from leaving cooked rice warm/at room temperature for too long, because some bacteria (like Bacillus cereus) can grow and sometimes produce toxins.

So the practical rule is simple: cool it fast, chill it cold, and handle it cleanly.

Practical takeaways (simple + useful):

Want to eat rice tomorrow? Do this: cool it within 1–2 hours, put it in a clean box, and store it in the fridge (~4°C).

Make it cool faster: spread rice on a wide plate/tray for a few minutes, then pack it.

Reheat plain rice properly: reheat until it’s steaming hot all the way through, then eat.

Don’t keep moving it in and out: fewer temperature changes = safer.

❌ Don’t leave cooked rice out for long (especially in hot Indian weather).

❌ Don’t rely on smell/taste food can look normal and still be risky.

Curd rice isn’t a preservation hack: curd makes it more acidic and sour with time, but it doesn’t cancel the “time + temperature” rule. If you mix curd, keep it refrigerated and don’t leave it out.

Disclaimer: This information is for educational purposes only and is not health or medical advice

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More from @TejasTekk

Dec 14, 2025
In a rope pushdown, each arm doesn’t share the load equally.
The outward pull quietly increases the force.

If you're doing the two-handed rope pushdown for triceps, you're probably loading the cable with 20kg, you would expect 10 kg of load experienced by each end
But the actual force experienced by each hand is greater than half of the total cable weight.
Because you're not just pushing down you're pushing down and out.

More details below ⬇️
Your triceps are responsible for elbow extension.
Any exercise that challenges this motion will train the triceps.
Now in a double-hand rope pushdown, the direction of the cable resistance is downward but once you start pushing the rope outward at the bottom, things change.

You're now applying force in two directions:
Vertical (downward) — to oppose the cable weight.
Horizontal (outward) — to separate the rope ends and finish the rep in full extension

Let's say you're using 20 kg on the cable machine.

In a perfect vertical push (like with a straight bar or single-arm setup), each arm handles 10 kg.

But with a double-hand single rope, the ends of the rope move outward as you push down, forming an angle ‚let's assume 30° per side from vertical (total 60° between ropes).

Now you're not just pushing down, you're also pushing out.
Total load: 20 kg
Each rope side angled 30° from vertical

10/ cos 30º=11.55

Each arm ends up handling = 11.55 kg instead of just 10 kg.
That's about 15% more load per arm even though the cable stack still says 20 kg.

Single arm pushdown or using 2 long ropes instead of one can reduce the angle and make each rope hang more vertically, so the outward force drops and each arm handles closer to 10 kg, not 11.55

Rope angle makes a big difference
The more you pull the rope outward, the wider the angle becomes.
A wider angle means a bigger horizontal force, increasing the total force your arm has to produce.

This is especially tough at the bottom of the movement, when your elbows are fully extended and your triceps are in a weaker, shortened position. So it feels harder ,because it actually is.
Read 5 tweets
Dec 6, 2025
Want to live longer, think clearer, age slower, and dodge chronic disease?

Build muscle.

Not because it looks good,
but because every extra kilogram of muscle literally makes you harder to kill.

What the research shows

+1 kg of muscle → lower risk of death
People with the most muscle had a lower mortality than those with the least.

Low muscle = risk of age related brain disease risk
Smaller muscles = higher dementia risk
Sarcopenia nearly triples Alzheimer’s risk.
Muscle protects the brain.

Cancer? Muscle matters
Strength training = lower cancer risk
Losing lean mass increases cancer death risk

Heart health
More muscle = lower cardiovascular events
Your biceps may be better than your blood pressure meds.

Type 2 Diabetes
Strength training = lower diabetes risk
Muscle is where glucose goes. No muscle? No glucose control.

Why muscle is a longevity organ

Muscle releases myokines hormone-like signals that:

Reduce inflammation
Protect the brain
Improve insulin sensitivity
Support blood vessels
Boost metabolic health

The more muscle you have, the more of these protective molecules your body makes.

The crazy part
You don’t need dramatic gains.
Just +1% muscle per year (totally doable with strength training) compounds into massive risk reduction over a decade.
Small improvements → huge protection.
A major 2025 study people with higher lean body mass (i.e. more muscle/lean tissue compared to fat) had a significantly lower risk of developing type 2 diabetes
pubmed.ncbi.nlm.nih.gov/40551720/

Muscle is more than strength, It’s a metabolic organ
Your muscles don’t just move your body they protect your metabolism. When you strength train, your muscles release special hormones and signals that help your body manage sugar, burn fat, and use energy more efficiently. That means:
More muscle = better metabolic health
Less muscle = higher risk of obesity, insulin resistance, and type 2 diabetes
Doctors now recommend strength training not just for athletes, but as essential medicine for ageing well.

Introducing: Strengthspan
Just like lifespan is how long you live, strengthspan is how long you stay strong and functional. The longer your strengthspan, the more likely you are to:
Live independently, Avoid lifestyle diseases
,Maintain mobility as you age
and enjoy a higher quality of life
Strength isn’t something you should start worrying about at 65, it’s something you build now, little by little, and protect for life.

pubmed.ncbi.nlm.nih.gov/40784602/
pubmed.ncbi.nlm.nih.gov/38754987/
pubmed.ncbi.nlm.nih.gov/39948829
When the body
faces illness, injury, surgery, or any major stress, it draws on muscle to supply amino acids and proteins needed to:
* Repair damaged tissues
* Support the immune system
* Fight inflammation
* Maintain vital organs
Without this reserve, the body is forced to break itself down.

Why muscle matters during illness

ICU patients can lose 15–20% of their muscle in just one week.
That’s like aging several decades in days.
This massive muscle loss leads to:
❌ slower recovery
❌ prolonged weakness
❌ higher risk of complications
❌ poorer survival rates
But here’s the good news:
Patients who enter illness, surgery, or hospitalization with more muscle recover faster and experience up to 75% less long-term impairment months later.

sciencedirect.com/science/articl…
journals.sagepub.com/doi/10.1177/08…
Read 9 tweets
Nov 29, 2025
Air fryers: Are they safe?

Air fryers cook by rapidly circulating hot air, not oil around food. This initiates the Maillard reaction, which browns food and creates flavour.
Air frying uses significantly less oil than deep-frying, which reduces fat content.

(TLDR: Air-fryers are safe)

Here is a detailed post on this topic⬇️Image
Air fryers can help you make french fries with less oil and less calories still maintain crisp texture then
what is the concern?
The concern around airfryers is due to acrylamide formation.

Acrylamide is a Maillard byproduct formed during high heat cooking. Acrylamide isn’t an additive. It’s a natural byproduct formed foods undergo high-heat, dry cooking.
Acrylamide is classified as a probable human carcinogen (IARC Group 2A) based mainly on animal studies at extremely high doses
Most studies on fried potatoes show that air frying produces much less acrylamide than deep frying often 60–90% lower, especially when you also soak, blanch, or use plant-based pretreatments before cooking.

Air-fried fries and chips cooked around 170°C for 8–12 minutes generally have lower acrylamide and less oil, making them the healthier option.

One 2024 study seemed to show slightly higher acrylamide with air frying, but the levels were below the lab’s detection limit and far lower than typical values in the literature, so its results are considered unreliable and don’t overturn the broader evidence in favor of air frying.

Study review- comments on the study:
Reviewing the Study Claiming Higher Acrylamide in Air-Fried Potatoes
A study reported more acrylamide in air-fried potatoes than in deep-fried or oven-fried ones. However, several issues limit its reliability:
All acrylamide values were below the Limit of Quantification (LoQ), meaning they could be detected but not accurately measured or compared.
Reported levels were about 10× lower than what other studies typically find in fries and chips, suggesting methodological inconsistencies.
Soaking potatoes before deep frying reduced acrylamide to almost undetectable levels.
Sunflower oil used in the study may have caused minor cross-contamination, but levels were still unusually low compared to existing research.
Takeaway: The study’s acrylamide values are too low and imprecise to draw firm conclusions, so it should not overturn the broader evidence showing air frying generally produces less acrylamide than deep frying.

fppn.biomedcentral.com/articles/10.11…
ffhdj.com/index.php/ffhd…
pubmed.ncbi.nlm.nih.gov/25619624/
efsa.europa.eu/en/topics/topi…
pubmed.ncbi.nlm.nih.gov/32375322/
pubmed.ncbi.nlm.nih.gov/25872656/
frontiersin.org/journals/nutri…
mdpi.com/2304-8158/13/4…
pubmed.ncbi.nlm.nih.gov/33610846/

Comments on the study:
frontiersin.org/journals/nutri…

pubmed.ncbi.nlm.nih.gov/25619624/
efsa.europa.eu/en/topics/topi…
pubmed.ncbi.nlm.nih.gov/32375322/
pubmed.ncbi.nlm.nih.gov/25872656/
frontiersin.org/journals/nutri…
Read 8 tweets
Nov 23, 2025
Every single day, your body synthesizes approx. 200-300g of new protein to replace old or damaged proteins.
This turnover happens at different rates across tissues, your liver, muscles, and connective tissues are constantly renewing themselves.

Over the course of a year, you’ve effectively replaced nearly every protein in your body four times over.
Muscle accounts for ~50% of your body’s total protein, but only about 25% of the total turnover happens here.

The liver, on the other hand, has a much higher turnover rate because it constantly produces proteins for metabolism.

While carbohydrates (glycogen) and fats (triglycerides) have dedicated storage, there is no long-term storage for amino acids.
Instead, your body maintains a dynamic amino acid pool, but it only lasts for about 8 hours.
After that, your body must obtain new amino acids, either from dietary protein or by breaking down muscle tissue.
This constant flux is why regular protein intake is essential for maintaining muscle mass, enzyme function, and overall health.

Your body is always rebuilding give it the raw materials it need.

Here is everything you may need to know about protein, an extremely detailed post.
Proteins are made of amino acids
Your body needs 20 amino acids to function

Essential (9) → must come from diet
Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine

Conditionally Essential (6) → needed in stress/illness/growth or special conditions etc.
Arginine, Cysteine (from Methionine), Glutamine, Glycine, Proline, Tyrosine (from Phenylalanine)

Non-Essential (5) → usually made by the body
Alanine, Asparagine, Aspartic acid, Glutamic acid, Serine

The focus should be to get all essential amino acids in adequate amount by consuming adequate amount of protein (this will also help provide conditionally essential amino acids in good amount)
Protein RDA part-1

Why the protein RDA of 0.8g of protein per kg of bodyweight is not enough for most people.
For most people protein intake of 1.2-1.5g protein per kg of bodyweight is considered optimal.

The Recommended Dietary Allowance (RDA) for protein in adults is currently set at 0.8 g/kg/day. This value is not based on modern measures of muscle protein synthesis or health outcomes but rather on nitrogen balance studies conducted decades ago, often in young college students.

The science behind Protein RDA

Nitrogen balance method
Protein is the only macronutrient containing nitrogen.
Nitrogen balance measures the difference between nitrogen intake (from protein in food) and nitrogen losses (mainly urine urea, but also feces, sweat, respiration, hair, and skin).

Zero balance = intake equals loss → considered adequate.
The RDA is set at the intake needed to achieve zero nitrogen balance plus a safety margin.➝ Limitation: This method tells us only about net nitrogen retention, not whether protein intake optimizes health, muscle, or performance.
Read 21 tweets
Oct 18, 2025
Whey protein as a food supplement has gained significant traction in India over the past 5–10 years, but humans have been using whey for more than 200 years.

Whey protein’s story began long before supplements and shaker bottles ,nearly 8,000 years ago, around 5,500 BC in Kujawy, Poland.
Back then, early cheesemakers accidentally discovered that when milk was stored in animal stomachs or mixed with acidic plants, it separated into solid curds(cheese) and liquid whey.

For centuries, whey was mostly used as feed or a starter for cheese.
But around 460 BC, Hippocrates, the Father of Medicine, began prescribing whey (then called “serum”) for its healing properties treating liver disease, jaundice, and skin ailments.
This idea spread across ancient Greece and Rome whey as medicine.
Fast forward to the 17th and 18th centuries. Swiss farmers noticed their pigs fed on whey grew faster and healthier.

Soon after, whey became the centerpiece of European health resorts people didn’t just drink whey,they bathed in it, believing it rejuvenated skin, , and improved how they feel.

Whey spas thrived across Switzerland, Germany, and Austria a curious blend of rustic tradition and early wellness culture.

By the 1890s, scientists began isolating specific proteins from whey,lactalbumin and lactoglobulin.

By the 1930s, these proteins were successfully crystallized, paving the way for nutritional research that would change sports and health forever.

Today, we understand whey as one of the highest-quality complete proteins, rich in essential amino acids, rapidly absorbed, and scientifically proven to support muscle growth, recovery, and immune health.

What started as a humble cheesemaking byproduct is now a cornerstone of modern nutrition a symbol of how ancient wisdom and scientific discovery can align perfectly.
pubmed.ncbi.nlm.nih.gov/23235824/
milkgenomics.org/?splash=europe…
psu.edu/news/research/…
researchgate.net/profile/Michae…
physicalculturestudy.com/2015/12/07/a-p…
pmc.ncbi.nlm.nih.gov/articles/PMC71…
sciencedirect.com/science/articl…
Most people hear whey protein, they think of muscle recovery and fitness.
But this dairy protein quietly powers industries far beyond nutrition, from skincare to agriculture, pharmaceuticals, and even sustainable packaging.

1. Whey in skincare & cosmetics
Whey protein isn’t just good for your muscles it’s good for your skin.
Rich in amino acids, some high-end skincare brands use whey protein in:
•Moisturizers and sunscreens (for smooth, silky texture)
•Shampoos and hair products (for strengthening and shine)
•Pressed powders and lotions (for improved emulsion stability and pigment dispersion)

2. Fighting plant viruses
whey proteins can protect crops.
Fractions like α-lactalbumin, β-lactoglobulin, and lactoferrin have shown antiviral activity, they can inhibit the Tomato Yellow Leaf Curl Virus (TYLCV), one of the most damaging plant viruses.

3. Edible food packaging
Whey proteins are now being used to create biodegradable, edible films and coatings for food packaging.
These films form smooth, oxygen-resistant layers that preserve freshness, a sustainable alternative to plastic.

4. Pharmaceutical and medical applications
Whey proteins serve as encapsulation and emulsifying agents in modern drug delivery systems protecting sensitive compounds and improving bioavailability.
They’re also being studied for cancer therapy support, thanks to their antioxidant and immune-enhancing properties.

5. Baby food
Because of its high amino acid score and digestibility, whey protein isolate is a key ingredient in many infant formulas, medical nutrition products, and protein-fortified beverages.
Its amino acid composition closely resembles that of human milk making it ideal for early growth and recovery support.

6. Food Industry innovations
From yogurts and cheeses to ice creams, baked goods, soups, sauces, and confectionery, whey adds protein, texture, and emulsification stability.
It’s everywhere ,not just in your shaker bottle.

7. Biotechnology & sustainability
In biotechnology, whey acts as a fermentation substrate, producing valuable bioactives like:
•Organic acids
•Bacteriocins (natural antimicrobials)
•Exopolysaccharides (used in food and pharma)
•Enzymes and peptides for bioenergy and agriculture
Read 7 tweets
Sep 30, 2025
It is estimated that yeast protein can contain anywhere between 20–80 times higher purines than whey (depending on the strain and processing method)

Fermented yeast protein is a high-quality protein source with a complete amino acid profile, but yeast protein is a high purine protein source.

For most healthy individuals, moderate intake is safe. A practical guideline would be to limit total yeast protein intake to around 40–50 g per day (≈1–1.5 scoops),

For individuals with hyperuricemia or a history of gout, a more conservative limit is advisable: ≤20 g per day (≈0.5 scoop), since high purine intake can contribute to elevated uric acid levels.

Yeast protein can be included daily as part of a varied diet, but it should not be relied on as the sole or major protein source.
Saccharomyces cerevisiae is a protein-rich yeast, and the purines present can be metabolized to uric acid in humans. Studies show that consuming large amounts of yeast-derived single-cell protein (SCP), such as 30g/day, can significantly increase uric acid levels, especially in sensitive individuals.
Lower doses do not reliably cause uric acid elevation in healthy subjects.

Yeast protein contains purines (adenine, guanine) which, when metabolised, increase uric acid production in the body.

Most controlled studies do not show adverse uric acid effects in healthy populations.

High intake or regular use in those predisposed (gout, chronic hyperuricemia) could exacerbate uric acid buildup.

Fermented yeast protein purine content varies by strain, fermentation method, and extraction. Non-probiotic S. cerevisiae typically contains 300–600 mg/100g, while nutritional yeast is at the lower end (~150mg/100g).

Whey protein isolate is safe for those at risk of hyperuricemia due to its negligible purine content.

For yeast protein, moderate daily intake (<30g) is unlikely to significantly elevate uric acid in healthy individuals, but higher dosages, especially more than 30g/day and above, can raise uric acid levels, notably in those with impaired purine metabolism.

Individuals with gout or chronically high uric acid should avoid regular fermented yeast protein or dramatically limit intake.

Typical yeast protein (Saccharomyces cerevisiae) contains about 150–600 mg purines per 100g.

Purine content per serving could be 54–216 mg purines.

Most food-grade, fermented yeast proteins are processed to reduce purine content, but unless labelled as "low purine" or specifically purified, the lower estimate 50–100 mg purines per scoop
Whey protein isolate is a low purine protein source

Purines in whey -0–10 mg/100 g (≈0–3 mg per 30 g scoop).

Essentially negligible → dairy is classified in the lowest purine group.

Safe for gout / hyperuricemia, often considered “Extremely low purine” in guidelines.
Fermented Yeast Protein

Purines- ~285 mg/100 g for nutritional yeast.
some yeast proteins (brewer’s yeast, extracts): 300–847 mg/100 g.

That could be approx. 20–85× more purines than whey isolate.

For people with gout, daily purines are usually limited to <200 mg.
Why so high in yeast?
Yeast cells are rich in RNA/DNA → purine nucleotides.

fermented yeast protein alone does not directly cause elevated uric acid levels. Uric acid accumulation depends on the total dietary purine load, overall calorie balance, alcohol intake, fructose consumption, and other lifestyle/dietary factors. Yeast protein is high in purines, but when consumed in moderation and as part of a balanced diet, it can safely contribute to daily protein needs.

Yeast can be a great source of protein but best to combine different protein sources to complete your protein requirement
Read 8 tweets

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