Studies on proteolytic inhibitory peptides from the seeds Ricinus communis

Abstract

The search for dietary compounds that prevent many life style diseases is deemed crucial to tackle this major health problem worldwide, and recent developments in the field of health have suggested that increased protein consumption, particularly from plant sources, might reduce many life style diseases. Nowadays, interest among researchers has been emerging to identify, isolate and characterize bioactive peptides from plant and animal sources. Bioactive peptides are considered as specific protein fragments that are inactive within the sequence of the parent protein and they exhibit various physiological functions after released from their parent protein. Bioactive peptides were produced by germination, fermentation and cold storage from the seeds of Ricinus communis. The seeds were germinated for various days and germinated seedlings were subjected to fermentation for different period of time using Bacillus substilis.  The total protein and protease inhibitor activity were monitored during germination. The fermented soluble protein content was further subjected to cold storage (0 – 4^oC) for seven days. The protein content was gradually increased from first day of germination (9.18%) and it was maximum on the third day (11.73%) followed by gradual decrease their onwards. It was observed that proteolytic inhibitory activity was less  in the initial period of germination (23.32 TIU/mg of protein) followed by gradual increase up to fourth day (32.04  TIU/mg of protein) and decrease their onwards during the germination. Similarly, fourth day Fermented and fifth day cold stored sample showed high proteolytic inhibitory activity, 408 TIU/mg and 286 TIU/mg respectively.