The proteins in potato fruit juice represent a very large pool of non-exploited ingredients for human consumption. The worldwide production of potato starch releases millions of cubic meters of potato juice containing about one percent highly functional, bioactive and nutritious proteins.
The current industry practice is to separate this protein by heating and/or acidic precipitation techniques. This result in less desirable products as these processes destroy the native characteristics of the proteins with poor solubility and palatability as the result.
Our Controlled Affinity Separation (CAS) techniques have proven very efficient in isolating the major protein fractions of patatin and protease inhibitors from crude potato fruit juice either as a bulk protein isolate or as refined individual proteins with distinct functionalities.
Our development and application work focus on patatin and proteinase inhibitor based ingredients exhibiting desirable color, taste and functional properties in a broad range of food applications.
Patatin is a group of glycoproteins having a molecular weight from 40 to 45 kDa representing approximately 40 % of the total soluble protein in potato fruit juice.
Patatin has the same nutritional profile as egg albumin and has excellent emulsifying and gelling properties. Native patatin further possess enzymatic activity as a lipid acyl hydrolase and acyl transferase which may be utilized in certain food applications.
Protease inhibitors are the second most abundant group of proteins found in potatoes. They possess molecular weights in the range of 5 to 25 kD and constitutes 30-40 % of the total soluble protein in potato fruit juice.
The potato protease inhibitors have excellent foaming and gelling properties. In addition, their ability to inhibit proteases may be applied for preserving texture and taste profiles.