Advances in Microbial Physiology, Vol. 24 by A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.)

By A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.)

This quantity in a research-level sequence covers various points of microbial body structure and biochemistry together with inositol metabolisms in yeasts, bacterial adhesion, natural acids, the bacterial flagellum and the mechanical behaviour of bacterial mobilephone partitions. it's meant to be of use to microbiologists, biochemists and biotechnologists. different similar works during this sequence are volumes 29, 30 and 31.

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Extra resources for Advances in Microbial Physiology, Vol. 24

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From Egli et nf. (1980). dilution rate the residual glucose concentration in the Kloeckera cultures was significantly higher than in the Hansenula culture. This observation may explain how it was that in the Kloeckera culture derepression of synthesis of alcohol oxidase was accomplished only at much lower dilution rates than in H. polymorpha. Synthesis of alcohol oxidase and catalase in the two organisms was also investigated during growth on mixtures of methanol and glucose in continuous culture.

In (c) and (f) . . , . indicates productivity of alcohol oxidase during growth on methanol as the sole source of carbon. Productivity is expressed as units (pmol min-' mg-' h-l), alcohol oxidase as pmol oxygen consumed min-' (mg protein)-' and catalase activity as AA24 min-' (mg protein)-'. From Egli (1980). physiological function (Eggeling and Sahm, 1980). , 1980). It may be envisaged that this exogenous glucose in turn is in equilibrium with intracellular metabolites derived fi;om glucose which initiate the onset of 46 M.

32 M. I. P. VAN DIJKEN AND W. HARDER In bacteria, several different enzymes have been found that catalyse the oxidation of methylated amines (Large, 1981). These include various mono-oxygenases, dehydrogenases and oxidases. , an organism that can utilize this compound as a nitrogen source, has been investigated by Yamada et al. (1966). They showed that in this organism methylamine was metabolized by way of a primary amine oxidase which oxidized it to formaldehyde and ammonia. Methylamine was not a specific substrate for this enzyme which also catalysed the oxidation of various primary amines according to the equation: Hz R-C-NH~ H I +H ~ +O02+R-C=O +H ~ +ON H~ ~ (9) The activity of the enzyme towards alkylated amines decreased with increasing chain length of their molecules.

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