식품단백질의 효율적인 이용을 위하여 neutrase에 의한 glutamine과 asparagine 잔기의 탈아미드화에 관한 연구를 행하였다. Neutrase에 의한 BSA의 최적반응 조건은 $20^{circ}C$, pH 10에서 3시간 반응시켰을 때로, 이때 BSA는 24%가 탈아미드화되었고. 동시에 2.9%가 가수분해되었다. 또한 pronase, bromelain, ficin 보다는 neutrase에 의한 BSA의 탈아미드화율이 높은 것으로 나타났다. 최적 탈아미드화 조건에서 neutrase에 의한 egg albumin, 분리콩단백 및 casein의 경우 탈아미드화에 수반하여 펩티드결합의 분해가 비교적 높게 관찰되었다.
Deamidation by neutrase on glutaminyl and asparaginyl residues of protein was examined. The optimum pH and temperature for BSA(bovine serum albumin) deamidation by neutrase were 10 and $20^{circ}C$, respectively. The incubation for 3 hrs under the optimum condition removed 24% of amide groups and hydrolyzed 2.9% of peptide bonds. Deamidation by neutrase was superior to that by pronase, bromelain, or ficin. Deamidation degrees of egg albumin, soy protein isolate and casein by neutrase under the optimum condition were about 20%, 14% and 14%, respectively. However, relatively high degree of peptide hydrolysis was accompanied with casein deamidation.
