Gellissen G, Piontek M, Dahlems U, Jenzelewski V, Gavagan J E, DiCosimo R, Anton D L, Janowicz Z A
Rhein Biotech GmbH, Düseldorf, Germany.
Appl Microbiol Biotechnol. 1996 Aug;46(1):46-54. doi: 10.1007/s002530050781.
The methylotrophic yeast Hansenula polymorpha has been developed as an efficient production system for heterologous proteins. The system offers the possibility to cointegrate heterologous genes in anticipated fixed copy numbers into the chromosome. As a consequence co-production of different proteins in stoichiometric ratios can be envisaged. This provides options to design this yeast as an industrial biocatalyst in procedures where several enzymes are required for the efficient conversion of a given inexpensive compound into a valuable product. To this end recombinant strains have been engineered with multiple copies of expression cassettes containing the glycolate oxidase (GO) gene from spinach and the catalase T (CTT1) gene from S. cerevisiae. The newly created strains produce high levels of the peroxisomal glycolate oxidase and the cytosolic catalase T. The strains efficiently convert glycolate into glyoxylic acid, oxidizing the added substrate and decomposing the peroxide formed during this reaction into water and oxygen.
多形汉逊酵母已被开发成为一种用于生产异源蛋白的高效系统。该系统提供了将异源基因以预期的固定拷贝数共整合到染色体中的可能性。因此，可以设想以化学计量比共同生产不同的蛋白质。这为将这种酵母设计成工业生物催化剂提供了选择，在将给定的廉价化合物高效转化为有价值产品的过程中需要几种酶。为此，构建了重组菌株，这些菌株含有多个表达盒拷贝，其中包含来自菠菜的乙醇酸氧化酶（GO）基因和来自酿酒酵母的过氧化氢酶T（CTT1）基因。新构建的菌株产生高水平的过氧化物酶体乙醇酸氧化酶和胞质过氧化氢酶T。这些菌株能有效地将乙醇酸转化为乙醛酸，氧化添加的底物，并将该反应过程中形成的过氧化物分解为水和氧气。
