The role of gene polymorphisms of glutamate-cysteine ligase catalytic (GCLC) enzyme against antioxidants and oxidative stress status of Individual who had contacted infectious tuberculosis

Aims: Glutamate cysteine ligase (GCL) enzyme is involved in the synthesis of glutathione, which functions as an antioxidant. Polymorphisms in the sequence of amino acids making up the gene GCLC will cause differences in enzyme expression and GCLC activity. Gene expression that is influenced by oxidative stress can be used to measure markers such as F2-isoprostanes. This study aims to examine the association between the polymorphism in the GCLC gene with glutathione plasma level and F2-isoprostanes in contacts of person with infectious tuberculosis (TB). Methodology and results: Samples are taken from the family members of pulmonary TB patients who seeks treatment at the Pulmonary Centre (Lung Health Center for Public = BBKPM) and Policlinic of Dr Wahidin Sudirohusodo Hospital, Makassar. Total of approximately 4 mL of venous blood are taken from each person with pulmonary TB contacts and furtherly analyzed using genomic PCR-RFLP method and ELISA. Our results described that contacts of person with infectious TB for approximately 6 months have polymorphism C/C genotype at 80.3%, C/T of 18.3% and T/T for 1.4% of the total 71 samples with high levels of glutathione from 0.167 to 0.548 mM/mL and F2-isoprostanes level 72.4 - 1343.9 pg/mL. Conclusion, significance and impact of study: There are no significant association between GCLC gene polymorphism with glutathione and F2-isoprostanes levels of individual who had contacted infection TB. In this study the elevation of F2-isoprostanes equal to the decrease levels of glutathione.

Selection of Chitinolytic Bacteria as Biological Control of Colletotrichum capsici

Aims: The objectives of this study were to screen chitinolytic bacteria isolated from soil of Taman Nasional Bukit Duabelas, Jambi, Indonesia. Isolates were selected based on chitinolytic index and antagonism activity of Colletotrichum capsici. Chitinase enzyme from selected isolates was investigated for growth inhibition of C. capsici. Methodology and results: Two chitinolytic bacteria were selected based on their ability to degrade colloidal chitin and inhibit of the growth of C. capsici. Those isolates were KAHN 15.12 and SAHA 12.12, identified as Serratia marcescens and Bacillus thuringiensis respectively based on 16S rRNA gene. The chitinase maximum specific activity of isolate KAHN 15.12 was 52.03 U/mg after 36 h of incubation and SAHA 12.12 was 45.67 U/mg after 24 h of incubation. The enzyme was precipitated by ammonium sulfate 40% and 60% respectively for KAHN 15.12 and SAHA 12.12. The precipitated chitinases were active over a broad range of pH (5 to 10) and temperature (20 to 80 °C). Enzymes were stable in optimum temperature for 180 min. The precipitated of chitinase KAHN 15.12 and SAHA 12.12 had five and two protein bands respectively on SDS-PAGE gel. Chitinases exhibited an antifungal activity against C. capsici at concentration of 60 ppm. Conclusion, significance and impact of study: Isolates KAHN 15.12 and SAHA 12.12 were successfully selected by their ability to degrade colloidal chitin and inhibit the growth of C. capsici. The isolates had a broad range of pH and temperature, moreover relatively stable at the optimum temperature. Chitinase was effective as biological control for anthracnose caused by C. capsici in chilli.