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 varied features 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 mobile 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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These results exclude the possibility of staining of the organelles as a result of diffusion of hydrogen peroxide, generated by the oxidase, from the cytoplasm into the organelle since this would have resulted in staining at the periphery of the organelles. , 1976). e. the same procedure applied to unjixed cells or in the presence of aminotriazole) demonstrating that catalase activity is really present in the originally unstained parts. Taken together these results suggest that after incubations with diaminobenzidine/methanolthe diaminobenzidine reaction product is only formed at the sites of alcohol oxidase activity.

1 h-' and to a much smaller extent than in H. polymorpha. The extent of repression of synthesisof alcohol oxidase in both organisms is most likely a function of the residual glucose concentration in the culture. This concentration was estimated for both organisms at different dilution rates and was found to fit the equation: S = Ks. 51 h-' for H. 42 h-' for Kloeckera sp. 2201. These data show that at a certain M. VEENHUIS, J. P. VAN DIJKEN AND W. 5 Dilution rate (h-') FIG. 20. Alcohol oxidase (pmol 02 consumed min-' (mg protein)-') and catalase (A& min-' (mg protein)-') activities in Hansenula polymorpha and Kloeckera sp.

This possibility was investigated in detail by Egli (1980) and by Egli et al. (1980) in the yeasts H. polymorpha and Kloeckera sp. boidinii). e. 3 - P 0 E L 2 10 20 30 40 50 60 70 Time ( h ) FIG. 19. 5% glucose and 1% methanol. Enzyme units as given in Fig. 18. From Sahm (1977). catalase was found at low dilution rates, although the extent to which derepression occurred was different for the different enzymes and organisms. In H. polymorpha alcohol oxidase activity in the cells increased with decreasing dilution rates (Fig.

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