as a Platform for Heterologous Expression of Enzymes Used for Industry.

In the 1980s, was the preferred host for heterologous protein expression owing to its capacity for rapid growth in complex media; well-studied genetics; rapid and direct transformation with foreign DNA; and easily scalable fermentation. Despite the relative ease of use of for achieving the high expression of many recombinant proteins, for some proteins, e.g.

Heterologous Expression of Extracellular Proteinase pAsPs of in .

Neutral protease pAsPs gene was obtained by sequence optimization of NpI protease from pAsPs was for the first time integrated in the genome of yeast strain T07, and then produced in a 5 L bioreactor with an enzyme yield of 150,800 U/mL of culture liquid towards casein. The specific activity of the pAsPs was 7,657,000 U/mg toward casein, 2320 U/mg toward hemoglobin, and 25,344 U/mg toward azocasein per 1 mg of the protein. The enzyme was found to be inhibited by Cu.

Heterologous Expression of Xylanase xAor from Aspergillus oryzae in Komagataella phaffii T07.

Xylanases (EC 3.2.1.