You are here:

Chemistry (including Biochemistry)/hydrolyzed keratin and formaldehyde


Hello, i have a 32oz bottle of 100% pure hydrolyzed keratin protein. I intend on using it on my hair as a keratin treatment. Do I need to dilute it before I use it.? I will clarify my hair, blow dry it, then apply the keratin and let it sit for about 20 min then blow dry , never rinsing it out. I am trying to duplicate a Brazilian keratin treatment. Once blow dried heat of 430 degrees will be applied via a flat iron to seal it in. Can I use the keratin in its pure state? Or do I need to dilute?

Also I am trying to duplicate the Brazilian blow out solution for a science experiment so if I want my 32oz bottle to contain 10 to 14% formaldehyde what kind and % should I use for the entire bottle? Also do I need to dilute the keratin and formaldehyde solution. I am basically trying to make a Brazilian style keratin treatment for the experiment.

Will the formaldehyde lose its strength in the keratin if not used in a certain amount of time?

The formaldehyde used in Brazilian keratin treatments, is it the same as the kind used in to preserve frogs etc...?

Please let me know what I need to use to duplicate a Brazilian styled keratin treatment.

Thank you,

Stumped chemistry student


l have good news and bad news.

The good news: One, you should MOST CERTAINLY DILUTE IT. (100% keratin was probably expensive, no?)

The bad news. If you live in the USA, you should know that the FDA doesn't actively police what goes into makeup the way they do in foods.

Makeup companies, skin care companies, and hair care companies aren't required to put the percentages of whatever on the bottle, or even report them ... unless there are potentially hazardous chemicals in there.

This means that legally you can say that your shampoo has keratin in it, even if the AMOUNT of actual keratin is around 1% or less.

Other than getting a salon bottle of keratin solution and running it through an analysis, I don't have a way to tell you how much keratin is in it.

Things I can tell you: Keep your bottle of keratin in the fridge for sure, tightly sealed. Keratin is a protein, and we want to keep it fresh so you can use it. Heat and oxidation will fry your protein.

See if you can get small locks of human hair as test swatches for your keratin. I'd make up a 1%, 2.5%, and 5% keratin solution and try those on your test swatches to analyze your results. You may find you can go down to a 0.5% solution or lower. (note: don't dilute all of your concentrated keratin. Just enough for the test, in case you find you need to go higher.)

As for formaldehyde, you'll have to find a reporter reaction for formaldehyde response and use that. I'm sure there are colorimetric assays or kits out there. :)

And yes, 100% formaldehyde is what is used to preserve frogs. :)

Chemistry (including Biochemistry)

All Answers

Answers by Expert:

Ask Experts


Trista Robichaud, PhD


No homework questions, especially ones copied and pasted from textbooks. I will answer questions about principles or give hints, but I do not do other's homework. I'm comfortable answering basic biochemistry, chemistry, and biology questions up to and including an undergraduate level of understanding. This includes molecular biology, protein purification, and genetics. My training/inclination is primarily in structural biology, or how the shapes of things affect their function. Other interests include protein design, protein engineering, enzyme kinetics, and metabolic diseases such as cancer, atherosclerosis, and diabetes. My chemistry weaknesses are that I do not know organic or inorganic synthesis well, nor am I familiar with advanced inorganic reactions. I will attempt quantum mechanics and thermodynamics questions, but primarily as they relate to biological systems. Furthermore, I cannot tell you if a skin photograph is cancerous, or otherwise diagnose any disease. I can tell you how we currently understand the basic science behind a disease state, but I cannot recommend treatment in any way. Please direct such questions to your medical professional.


I hold a PhD in Biomedical Science from the University of Massachusetts Medical School in Worcester. I specialize in Biochemistry, with a focus on protein chemistry. My thesis work involved the structure and functions of the human glucose transporter 1. (hGLUT1) Currently I am a postdoc working in peptide (mini-protein) design and enzymology at the University of Texas Health Science Center in San Antonio, Texas. I am in Bjorn Steffensen's lab (PhD, DDS), studying gelatinase A and oral carcinoma.

2001 American Association for the Advancement of Science
2007 American Chemical Society
2007 Protein Society
2011 UTHSCSA Women’s Faculty Association

Levine KB, Robichaud TK, Hamill S, Sultzman LA, Carruthers A. Properties of the human erythrocyte glucose transport protein are determined by cellular context. Biochemistry 44(15):5606-16, 2005. (PMID 15823019)
Robichaud TK, Appleyard AN, Herbert RB, Henderson PJ, Carruthers A “Determinants of ligand binding affinity and cooperativity at the GLUT1 endofacial site” Biochemistry 50(15):3137-48, 2011. (PMID 21384913)
Xu X, Mikhailova M, Chen Z, Pal S, Robichaud TK, Lafer EM, Baber S, Steffensen B. “Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2)” Matrix Biol. 2011 Sep;30(7-8):404-12. (PMID: 21839835)
Robichaud TK, Steffensen B, Fields GB. Exosite interactions impact matrix metalloproteinase collagen specificities. J Biol Chem. 2011 Oct 28;286(43):37535-42 (PMID: 21896477)

Poster Abstracts:
Robichaud TK, Carruthers. A "Mutagenesis of the Human type 1 glucose transporter exit site: A functional study." ACS 234th Meeting, Boston MA. Division of Biological Chemistry, 2007
Robichaud TK, Bhowmick M, Tokmina-Roszyk D, Fields GB “Synthesis and Analysis of MT1-MMP Peptide Inhibitors” Biological Chemistry Division of the Protein Society Meeting, San Diego CA 2010
Robichaud TK; Tokmina-Roszyk D; Steffensen B and Fields GB “Catalytic Domain Exosites Contribute to Determining Matrix Metalloproteinase Triple Helical Collagen Specificities” Dental Science Symposium. UTHSCSA 2011
Robichaud TK; Tokmina-Roszyk D; Steffensen B and Fields GB “Exosite Interactions Determine Matrix Metalloproteinase Specificities” Gordon Research Conference on Matrix Metalloproteinase Biology, Bristol RI 2011

Oakland University, Auburn Hills MI BS, Biochemistry 1998
University of Massachusetts Medical School, Worcester MA PhD, Biochemistry & Molecular Pharmacology 2001-2008
University of Texas Health Science Center, San Antonio TX Postdoc, Biochemistry 2009-Present

Awards and Honors
1998 Honors College Graduate, Oakland University
2009 Institutional National Research Service Award, Pathobiology of Occlusive Vascular Disease T32 HL07446
2011 1st Place, Best Postdoctoral Poster, Dental Science Symposium, UTHSCSA, April 2011

Past/Present Clients
Invited Seminars:
Robichaud TK, Fields GB. “Synthesis and Analysis of MTI-MMP Triple Helical Peptide Inhibitors” Pathology Research Conference, University of Texas Health Science Center San Antonio Pathology Department (June 18th, 2010)
Robichaud TK & Hill, B “How To Give A Great Scientific Talk” Invited Lecture, Pathobiology of Occlusive Vascular Disease Seminars, UTHSCSA (Nov 11th 2010), Cardiology Seminar Series, Texas Research Park (Feb 21st, 2011)
Robichaud TK; Tokmina-Roszyk D; Steffensen B and Fields GB “Exosite Interactions Determine Matrix Metalloproteinase Specificities” Gordon-Keenan Research Seminar “Everything You Wanted to Know About Matrix Metalloproteinases But Were Afraid to Ask” Bristol, RI (Aug 6th, 2011)

©2017 All rights reserved.