Construction of a plasmid for expression of glycosylated bovine beta-casein in Aspergillus oryzae.

Todd Z. DeSantis, Gabe Overbay, Rafael Jimenez-Flores, Susan Elrod.


Beta-casein is a non-glycosylated, monomeric milk phosphoprotein with a hydrophilic domain in its N-terminal region and a contrasting hydrophobic domain at its C-terminal end. This amphiphilic property makes beta-casein a good surface active agent that has applications in the food industry as well as the potential for use in biodegradation of marine petroleum spills. The bovine beta-casein gene has been previously cloned and mutated to contain a novel glycosylation site at Asn,3, near the N-terminus. This glycosylated protein has been shown to possess enhanced emulsifiying properties. It has also been demonstrated to act as an antifreeze agent. Previous attempts to produce enough protein for further study have not been very successful. Expression in a transgenic mouse system yielded 2 mg/ml, however the high cost of maintaining this system makes it impractical. Expression in a Pichia yeast system yielded

abstract No: 

Fungal Genet. Newsl. 46 (Supl):

Full conference title: 

Fungal Genetics Conference 20th
    • Fungal Genetics Conference 20th (1999)