Studies on Heated Protein Quality Using Homoarginine Method

다국어 초록 (Multilingual Abstract)

To determine the quality of heated protein, in vitro method, including lysine, lysinoalanine, and fructoselysine as well as homoarginine by guanidination of lysine, was assessed using heated casein with or without glucose. In vivo methods such as PER, digestibility and BV were also tried on homoarginine, lysinoalanine, fructoselysine, and lysine. The nonreactive lysine for guanidination was hardly digestive, while the non heat damaged lysine side chains in the protein were accessible for guanidination as well as for the digestion. A linear correlation(r=0.80) was obtained between PER and digestibility of the analysed lysine. Digestibility of homoarginine was higher than that of true protein. However, in the guanidinated heated casein with glucose, digestibility of homoarginine was significantly reduced. It is suggested that the homoarginine method may mislead to over- or underestimation of the damaged protein quality.

목차 (Table of Contents)

• Abstract
  
• INTRODUCTION
  
• MATERIALS AND METHODS
  
• RESULTS
  
• DISCUSSION
  
• ACKNOWLEDGMENTS
  
• REFERENCES