Right seat-side preference in a cinema has been explained by suggesting that it allows for emotional information processing by the right hemisphere (Karev, 2000). In order to determine seat-side preferences, participants in our experiments had to choose seats on cinema, theatre, and restaurant maps. The maps varied with respect to cinema screen, theatre stage, and restaurant entrance positions as viewed by the participants: on top, to the right, to the left, and at the bottom. Seat-side preference was found to be modified by the map's arrangement: With screen, stage, or entrance on top, participants preferred seats to the right of the screen, stage, or entrance, while for the other positions the results were not conclusive. Based on these results it cannot be concluded that the preference for a cinema seat is solely mediated by the preparation for an upcoming event to optimise emotional processing by the right hemisphere. Rather, seat choice seems to be determined by basic behavioural tendencies, such as which side to turn to when entering a room, or by visual attentional orientation.

A hybrid-immobilization method was developed to improve the long-term stability of laminaribiose phosphorylase immobilized on epoxy supports Sepabeads EC-EP/S. Entrapment in chitosan retained all of the enzyme activity depending on the amount of entrapped solid materials and increased half-life by a factor of 10-94.4 h. No enzyme activity loss was determined during 12 times reuse. The immobilization method is also applicable to sucrose phosphorylase immobilized on Sepabeads EC-EP/S. Up to 31.9 g/L laminaribiose were produced in bienzymatic batch experiments with reaction-integrated product separation by adsorption on zeolites.

Immobilization methods and carriers were screened for immobilization of Euglena gracilis extract with laminaribiose phosphorylase activity. The extract was successfully immobilized on three different carriers via covalent linkage. Suitable immobilization carriers were Sepabeads EC-EP/S and ECR 8209M with epoxy groups and ECR 8309M with amino groups as functional units. Immobilization on Sepabeads EC-EP/S resulted in highest retained activity (65%). The immobilizates were characterized for pH, temperature, and buffer molarity preferences. The immobilized enzyme lost 48% of its activity when used seven times. Together with sucrose phosphorylase, laminaribiose phosphorylase was successfully applied for bienzymatic production of laminaribiose from sucrose and glucose with a final laminaribiose concentration of 14.3 ± 2.1 g/L (20% yield).

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The diffusion of glucose and sucrose was investigated in membrane and bead experiments. Concentration-dependent diffusion coefficients of pure glucose and sucrose were determined in precipitated chitosan membranes of varying thickness using diffusion cell experiments. Contrary to fructose, the resulting diffusion coefficients of glucose and sucrose did not reach their free diffusion coefficients at infinite dilution suggesting additional interactions between chitosan and these two sugars. Counter-diffusion in bead experiments showed a good agreement between predicted and measured data allowing the inclusion of the diffusion data in the simulation of the proposed production process for laminaribiose. In conclusion, the encapsulation in chitosan presented a good trade-off between increased mass transfer resistance as evaluated by the Thiele modulus and improved thermal stability and antibacterial activity.