Biological properties of Cu(II) complexes with α-alanine
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DESYATNIK, A., CHAPURINA, Liudmila, TURTA, Constantin, TIURINA, Janeta, BIVOL, Cezara, CLAPCO, Steliana, DVORNINA, Elena, LABLYUK, S.. Biological properties of Cu(II) complexes with α-alanine. In: The International Conference dedicated to the 55th anniversary from the foundation of the Institute of Chemistry of the Academy of Sciences of Moldova, 28-30 mai 2014, Chișinău. Chișinău, Republica Moldova: Institutul de Chimie al AȘM, 2014, p. 69.
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The International Conference dedicated to the 55th anniversary from the foundation of the Institute of Chemistry of the Academy of Sciences of Moldova 2014
Conferința "The International Conference dedicated to the 55th anniversary from the foundation of the Institute of Chemistry of the Academy of Sciences of Moldova"
Chișinău, Moldova, 28-30 mai 2014

Biological properties of Cu(II) complexes with α-alanine


Pag. 69-69

Desyatnik A.1, Chapurina Liudmila2, Turta Constantin2, Tiurina Janeta1, Bivol Cezara1, Clapco Steliana1, Dvornina Elena1, Lablyuk S.1
 
1 Institute of Microbiology and Biotechnology of the ASM,
2 Institute of Chemistry of the Academy of Sciences of Moldova
 
 
Disponibil în IBN: 22 ianuarie 2019


Rezumat

Currently, the intensive researches to find new biologically active substances are conducted. The coordination compounds of copper (II) with α-amino acids, in particular with glycine and α-alanine, are one of the perspective classes of substances, that have proven important physiological action. They possess antitumoural, antiviral and antimicrobial properties. The stimulatory effect of these compounds on the growth and productivity of microalgae, cultivated for industrial application, as well as on biosynthesis of pectinases by Rhizopus arrhizus and lipases by Aspergillus niger, was demonstrated. The aim of the presence research was to investigate the effect of the copper (II) metal compounds with various stereoisomers of alanine: Сu(L-α-Ala)2 (1), Cu(DL-α-Ala)2·H2O (2), Cu(DL-α-Ala)2 (3), Cu(D-α-Ala)2 (4) on enzyme biosynthesis of Aspergillus niger CNMN FD 10 – producer of cellulases (cellobiohydrolase, endoglucanase, β-glucosidase) and xylanases, and Trichoderma koningii Oudemans CNMN FD 15 – producer of acid and neutral proteases. The complexes to the nutrition medium, in concentrations of 5, 10, 15mg/L were added. The enzymatic activity of the strain cultivated on the nutritive medium without metal complexes served as control sample. The cellulolytic and xylanolytic activity of the producer by method of Somogy-Nelson was determined. The proteolytic activity by modified method of Willstatter, using 5% gelatine solution as substrate, was assessed [1, 2]. Depending on type and concentration of metal complexes, the stimulatory effect was observed on day 7 for cellobiohydrolase and endoglucanase, being 6.67-66.67%, and 18.3726.24%, respectively, and on day 6 for xylanase, representing 36.30-52.51%. The coordination compounds indicated a neutral or inhibitory action on β-glucosidases. Studied compounds stimulated the activity of acid proteases with 45.81-54.19% on day 8 and activity of neutral proteases with 34.96-46.85% on day 9 of T. koningii growth. Optimal concentration of metal complexes was within narrow limits and presented 5-10mg/L for A. niger, and 10-15mg/L for T. koningii. Interest for biotechnology presents copper complexes 2 and 3 with racemic amino acid DL-α-Ala. They differ among themselves just in the presence of crystallization water molecule in structure of one of them. Thus, complex Cu(DL-α-Ala)2 can be used as stimulator of enzyme biosynthesis for micromycete A. niger; 5-10mg/L of the compound increased the activity of cellobiohydrolase with 66.67%, endoclucanase with 27.28%, xylanase with 31.53% and accelerated the endoglucanase and xylanase biosynthesis with 24 hours, while maintaining the activity of β-glucosidase at the control level. The coordination compound Cu(DL-α-Ala)2·H2O in concentration of 10-15mg/L presents perspective for T. koningii, demonstrating stimulatory effect of 31.93-26.67% on neutral protease and 46.85-44.75% on acid protease.