Peptidases and Trypsin Inhibitor in the Developing Endosperm of Opaque-2 and Normal Corn
1978
Reed, Carl | Penner, Donald
To determine the nature of the association of trypsin inhibitor content to lysine content in high-lysine corn (Zea mays L.), the relationship of proteolysis, trypsin inhibitor content, and lysine content was studied during endosperm development in opaque-2 and genetically similar normal corn. Peptidases with pH optima of 4.0, 5.5, 7.5, 8.4, and 10.0 capable of hydrolyzing α-N-benzoyl-dl-arginine-p-nitroanilide (BAPA) were extracted from the endosperm of developing field grown corn. These peptidases were inhibited by the endogenous trypsin inhibitor and were also unable to hydrolyze bovine albumin, wheat (Triticum aestivum L.) gliadin, zein, and Azocoll (Cal biochem general proteolytic substrate). Significant correlations were found between trypsin inhibitor content and dye binding capacity, a measure of lysine content, between trypsin inhibitor and pH 9.0 optimum peptidase, between the pH 9.0 optimum peptidase and lysine content, and between the pH 5.0 optimum peptidase and water-soluble protein content. Higher trypsin inhibitor levels found in opaque-2 corn were associated with higher albumin levels. Normal corn was lower in peptidase, lysine, trypsin inhibitor, and moisture than the genetically similar opaque-2 line.
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