화학공학소재연구정보센터
Enzyme and Microbial Technology, Vol.33, No.7, 926-931, 2003
Phosphatase production and activity in copper (II) accumulating Rhizopus delemar
The fungus Rhizopus delemar produced extracellular and cellular acid phosphatase during the growth in starch-supplemented medium in the presence or absence of copper ions. The levels of both AP-ase activities were maximal at the end of exponential growth phase and were dependent on copper concentrations. Copper ions in the medium provoked slight decrease of specific AP-ase activities and significant increase of the values of secreted enzyme per gram dry cells. On the other hand, an increase of copper ions in the reaction mixture leads to considerable increase of the values of cellular enzyme activity. Total uptake of copper (II) was highest at the highest copper (II) concentration, when resting cells were used. Between 27 and 30% copper (II) was not removed by acid washing, suggested that this copper was bound intracellularly by mycelium. Determination of the Michaelis constant for the cellular AP-ase gave value of 0.325 mM. The pH optimum of the enzyme was determined to be in the range of 3.5-4.5 using p-nitrophenyl phosphate (pNPP) as a substrate. The data obtained indicated a possible participation of AP-ases in the processes of heavy metal resistance and heavy metal uptake of this fungus. (C) 2003 Elsevier Inc. All rights reserved.