Extraction and characterization of chickpea (Cicer arietinum) albumin and globulin

Albumin and globulin fractions of 1 Desi and 2 Kabuli varleties of chickpeas (Cicer arietinum) were extracted with water and salt solutions (K2SO4 and NaCl). The extractable yields and particularly the albumin-globulin ratio varied greatly with the extraction medium and chickpea variety. Depending on the procedure employed, albumin could be extracted as a major fraction of chickpea proteins. Higher levels of essential amino acids and sulfur containing amino acids were found in albumins than in globulins of all chickpeas investigated. The common structural characteristics of both Kabuii and Desi chickpea albumins and globulins were clearly identified by densitometric profiles of their sodium dodecyl sulfate polyacrylamide gel patter: is. Albumins contained subunits with higher molecular weights than those of globulins. The in vitro digestibility of the chickpea proteins by papain, pepsin, chymotrypsin, and trypsin indicaed that globulins were more susceptible to proteolytic hydrolysis.