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Sweaty has already participated several times in RoboCup soccer competitions (Adult Size). Now the work is focused on stabilizing the gait. Moreover, we would like to overcome the constraints of a ZMP-algorithm that has a horizontal footplate as precondition for the simplification of the equations. In addition we would like to switch between impedance and position control with a fuzzy-like algorithm that might help to minimize jerks when Sweaty’s feet touch the ground.
BACKGROUND
Various neutral and alkaline peptidases are commercially available for use in protein hydrolysis under neutral to alkaline conditions. However, the hydrolysis of proteins under acidic conditions by applying fungal aspartic peptidases (FAPs) has not been investigated in depth so far. The aim of this study, thus, was to purify a FAP from the commercial enzyme preparation, ROHALASE® BXL, determine its biochemical characteristics, and investigate its application for the hydrolysis of food and animal feed proteins under acidic conditions.
RESULTS
A Trichoderma reesei derived FAP, with an apparent molecular mass of 45.8 kDa (sodium dodecyl sulfate–polyacrylamide gel electrophoresis; SDS-PAGE) was purified 13.8-fold with a yield of 37% from ROHALASE® BXL. The FAP was identified as an aspartate protease (UniProt ID: G0R8T0) by inhibition and nano-LC-ESI-MS/MS studies. The FAP showed the highest activity at 50°C and pH 4.0. Monovalent cations, organic solvents, and reducing agents were tolerated well by the FAP. The FAP underwent an apparent competitive product inhibition by soy protein hydrolysate and whey protein hydrolysate with apparent Ki-values of 1.75 and 30.2 mg*mL−1, respectively. The FAP showed promising results in food (soy protein isolate and whey protein isolate) and animal feed protein hydrolyses. For the latter, an increase in the soluble protein content of 109% was noted after 30 min.
CONCLUSION
Our results demonstrate the applicability of fungal aspartic endopeptidases in the food and animal feed industry. Efficient protein hydrolysis of industrially relevant substrates such as acidic whey or animal feed proteins could be conducted by applying fungal aspartic peptidases. © 2022 Society of Chemical Industry.
Significant improvements in module performance are possible via implementation of multi-wire electrodes. This is economically sound as long as the mechanical yield of the production is maintained. While flat ribbons have a relatively large contact area to exert forces onto the solar cell, wires with round cross section reduce this contact area considerably – in theory to an infinitively thin line. Therefore, the local stresses induced by the electrodes might increase to a point that mechanical production yields suffer unacceptably.
In this paper, we assess this issue by an analytical mechanical model as well as experiments with an encapsulant-free N.I.C.E. test setup. From these, we can derive estimations for the relationship between lay-up accuracy and expected breakage losses. This paves the way for cost-optimized choices of handling equipment in industrial N.I.C.E.-wire production lines.