Expression of the acid protease gene from Saccharomycopsis fibuligera in the marine-derived Yarrowia lipolytica for both milk clotting and single cell protein production.
In this study, the native acid protease gene in Yarrowia lipolytica 22a-2 with high content of protein was disrupted, and the disruptant 3-13-10 obtained had very low acid protease activity. Then, the acid protease gene (AP1 gene) from Saccharomycopsis fibuligera A11 was actively expressed in the disruptant 3-13-10, and the transformant 43 carrying the AP1 gene had high specific acid protease activity (46.7 U/mg). The recombinant acid protease produced by the transformant 43 was found to be able to actively clot milk, and the transformant 43 still kept high content of protein. The hydrolysis products of κ-casein under catalysis of the recombinant acid protease and the commercial calf rennet had the same molecular mass, suggesting that the recombinant acid protease and its producer can be used both in cheese manufacturing and as protein source in food industry.
UNESCO Chinese Center of Marine Biotechnology, Ocean University of China, Yushan Road, No. 5, Qingdao 266003, China.
Xin-Jun
XJ
Yu
Zhe
Z
Chi
Fang
F
Wang
Jing
J
Li
Zhen-Ming
ZM
Chi
Catherine
C
Madzak
D000818:Animals; D057055:Aspartic Acid Proteases / Q000235:genetics / Q000378:metabolism*; D004044:Dietary Proteins / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D008892:Milk / Q000382:microbiology*; D012442:Saccharomycopsis / Q000201:enzymology* / Q000235:genetics; D025062:Yarrowia / Q000201:enzymology* / Q000235:genetics
D004044:Dietary Proteins; D005656:Fungal Proteins; C012551:single cell proteins; D057055:Aspartic Acid Proteases