Kazuo Aisaka

Production of Lipoprotein Lipase and Lipase by Rhizopus japonicus

The distribution of lipoprotein lipase activity in microorganisms was examined, Rhizopus japonicus KY 521 showed the highest activity of lipoprotein lipase in the culture fluid among microorganisms tested, Lipase was also excreted in addition to lipoprotein lipase by this organism. The effect of cultural conditions on the extracellular production of the two lipases by this organism was investigated. The addition of phospholipid such as lecithin brought about a remarkable increase in the extracellular production of both lipases. It was found that lecithin did not increase significantly the net synthesis of the enzyme, but accelerated the secretion of the enzyme formed in the mycelium into the culture medium.

Properties of maltose phosphorylase from Propionibacterium freudenreichii

Abstract Maltose phosphorylase (EC 2.4.1.8) from Propionibacterium freudenreichii was purified and characterized. The enzyme ctalyzed both the phosphorolysis and the synthesis of maltose. In particular, in the synthetic reaction, the enzyme could use any of nine sugars other than d -glucose as a sugar acceptor, which resulted in the formation of new disaccharides, in which the first carbon of d -glucose and the fourth carbon of the other sugar were connected by an α-glycosidic linkage.

Hyperproduction of N-acetylneuraminate lyase by the gene-cloned strain ofEscherichia coli

SummaryOptimal culture medium for production ofN-acetylneuraminate lyase (NANA lyase) by the gene-cloned strain ofEscherichia coli, E. coli(pNALl), was screened to develop the process for the industrial production of NANA lyase. Out of nutrients tested, corn steep liquor (CSL) and sugarcane molasses were superior nutrient sources for the enzyme production. Hyperproduction (6–8 units/ml-broth) was achieved on the medium consisted of CSL and molasses.