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Jojoba seed meal proteins associated with proteolytic and protease inhibitory activities
Madan K Shrestha1, Irena Peri, Patricia Smirnoff
1Desert Plant Biotechnology Laboratory, Albert Katz Department of Dryland Biotechnologies, The Jacob Blaustein Institute for Desert Research, Ben-Gurion University of the Negev, Israel.
Abstract:
The jojoba, Simmondsia chinensis, is a characteristic desert plant native to the Sonoran desert. The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-inhibitory activity. SDS-PAGE showed two major proteins at 50 kDa and 25 kDa both in the albumins and in the globulins. The 25 kDa protein has trypsin- and chymotrypsin-inhibitory activities. In vitro digestibility of the globulins and albumins resembled that of casein and soybean protein concentrates and was increased after heat treatment. The increased digestibility achieved by boiling may be attributed to inactivation of the protease inhibitors and denaturation of proteins.