Lactalbumin hydrolysate

suitable for microbiology, Nutrient for fermentations and other applications

Peptone from lactalbumin
CAS Number:
EC Number:
MDL number:

Quality Level

biological source

bovine milk


≥11% total nitrogen (N) basis



shelf life

limited shelf life, expiry date on the label


microbiology: suitable (preparation)

ign. residue



≤6% loss on drying


6.8±0.5 (25 °C, 2% in H2O)


H2O: 2%, clear to very faintly turbid (light yellow to yellow and light brown-yellow to brown-yellow and light brown to brown)

Featured Industry

Food and Beverages

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General description

Lactalbumin contains high levels of essential amino acids.It is recommended for applications requiring a highly soluble source of amino acids and peptides. It is especially useful in fermentations, laboratory media and in tissue culture.

Other Notes

Sales restrictions may apply

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Monocyte chemotactic activity in human abdominal aortic aneurysms: Role of elastin degradation peptides and the 67?kD cell surface elastin receptor.
Hance, Kirk A., et al.
Journal of Vascular Surgery, 35 (2), 254-261 (2002)
Lesley Bell-Sakyi et al.
Experimental & applied acarology, 49(3), 209-219 (2009-03-03)
Primary cell cultures (n = 16) were initiated from tissues of embryonic and neonatal larval Ornithodoros moubata following methods developed for hard ticks. After maintenance for 20-25 months in vitro, cell multiplication commenced in surviving cultures, leading to the establishment...
Bertha Chen et al.
Fertility and sterility, 91(4 Suppl), 1351-1354 (2008-06-17)
We investigated the effect of relaxin on extracellular matrix remodeling in cultured myometrial compared with leiomyoma smooth muscle cells. Relaxin increases elastase activity and protease inhibitor expressions in myometrial smooth muscle cells, but no effect was observed in leiomyoma cells.
Hansen J Kosasih et al.
The Journal of biological chemistry, 291(7), 3197-3208 (2015-12-17)
The metalloproteinase ADAMTS-5 (A disintegrin and metalloproteinase with thrombospondin motifs) degrades aggrecan, a proteoglycan essential for cartilage structure and function. ADAMTS-5 is the major aggrecanase in mouse cartilage, and is also likely to be the major aggrecanase in humans. ADAMTS-5...

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