Concentration and Separation of Active Proteins from Potato Industry Waste Based on Low-Temperature Evaporation and Ethanol Precipitation.

Purpose. Potato fruit juice, a residue of starch industry, contains up to 2.5% [w/w] of proteins that are potentially valuable raw-materials of food, cosmetic, and pharma industries. The recovery of protein from the potato fruit juice is limited by the lack of industrially feasible concentration and separation technologies. The present research thus aimed at development of such process for the separation of active protease inhibitors from potato fruit juice. Methods. Low temperature mechanical vapor recompression evaporation was applied for concentration of potato fruit juice followed by ethanol precipitation for recovery of active proteins. The effects of precipitation temperature and precipitative agents were investigated employing response surface modeling methodology. Results. Concentration of potato fruit juice by evaporation was successful without loss of trypsin inhibition activity. Precipitation using 6.5 M ethanol at low temperature (0-+4°C) was found suitable for the recovery of active protease inhibitors from the concentrate. Piloting at starch industry yielded 50% of total proteins, with a high quantity of active protease inhibitors and a minor inclusion of other proteins. Conclusion. Concentration by low-temperature evaporation, followed by ethanol precipitation of protease inhibitors at optimized temperature, is an attractive option for valorization of potato fruit juice.

Screening of white-rot fungi manganese peroxidases: a comparison between the specific activities of the enzyme from different native producers.

In this study manganese peroxidase (MnP) enzymes from selected white-rot fungi were isolated and compared for potential future recombinant production. White-rot fungi were cultivated in small-scale in liquid media and a simplified process was established for the purification of extracellular enzymes.Five lignin degrading organisms were selected (Bjerkandera sp., Phanerochaete (P.) chrysosporium, Physisporinus (P.) rivulosus, Phlebia (P.) radiata and Phlebia sp. Nf b19) and studied for MnP production in small-scale. Extracellular MnP activity was followed and cultivations were harvested at proximity of the peak activity. The production of MnPs varied in different organisms but was clearly regulated by inducing liquid media components (Mn2+, veratryl alcohol and malonate). In total 8 different MnP isoforms were purified.Results of this study reinforce the conception that MnPs from distinct organisms differ substantially in their properties. Production of the extracellular enzyme in general did not reach a substantial level. This further suggests that these native producers are not suitable for industrial scale production of the enzyme. The highest specific activities were observed with MnPs from P. chrysosporium (200 U mg-1), Phlebia sp. Nf b19 (55 U mg-1) and P. rivulosus (89 U mg-1) and these MnPs are considered as the most potential candidates for further studies. The molecular weight of the purified MnPs was estimated to be between 45-50 kDa.