Open AccessEndogenous prolyl 4‐hydroxylation in Hansenula polymorpha and its use for the production of hydroxylated recombinant gelatin
Author(s) -
Bruin Eric C,
Werten Marc W.T.,
Laane Colja,
Wolf Frits A
Publication year - 2002
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2002.tb00047.x
Subject(s) - hydroxylation , biology , recombinant dna , biochemistry , heterologous , heterologous expression , yeast , endogeny , enzyme , gelatin , protein biosynthesis , gene
Several yeast systems have recently been developed for the recombinant production of gelatin and collagen. Amino acid sequence‐specific prolyl 4‐hydroxylation is essential for the gel‐forming capacity of gelatin and for the proper folding of (pro)collagen. This post‐translational modification is generally considered to be absent in microbial eukaryotic systems and therefore co‐expression of heterologous (human or animal) prolyl 4‐hydroxylase would be required. However, we found that the well‐known protein expression host Hansenula polymorpha unexpectedly does have the endogenous capacity for prolyl 4‐hydroxylation. Without co‐expression of a heterologous prolyl 4‐hydroxylase, both an endogenous collagen‐like protein and a heterologously expressed collagen fragment were found to be sequence‐specifically hydroxylated.