THE RELATIONSHIP BETWEEN SCHOOL WELL-BEING WITH ACADEMIC PROCRASTINATION OF STUDENTS IN SMP N 2 NGADIREJO

Nowadays students often postpone to start and finishing assignments or delay to finish assignments immediately. This study aims to examine the relationship between school well-being and academic procrastination. The sample in this study was 150 grade VIII students of SMP Negeri 2 Ngadirejo, Temanggung Regency, Central Java, who were selected by cluster random sampling technique. Data collection techniques using the school well-being scale and academic procrastination scale. Data analysis techniques using product moment correlation test. The results of Product Moment correlation analysis between school well-being variables and academic procrastination produce a correlation value (r) of -0.199 with a significant level of p = 0.015 (p <0.05). These results indicate that there is a significant negative relationship between school well-being and academic procrastination. This means that the higher the school well-being, the academic procrastination will be lower, conversely the lower the school well-being, the academic procrastination will be higher

Thermostable Lipase from Domestic Compost Isolated Bacteria

Lipase (Triacylglycerol acyl hydrolase), is a hydrolase enzyme that plays an important role in industries such as health, food, biotechnology, and energy. Lipase might be isolated from almost all living organism, either higher organisms or microbes. In this report, lipase was isolated from compost isolated microbe namely AL89 isolate. AL89 was previously identified closed to Pseudoxanthomonas taiwanensis. The crude extract of lipase was produced by incubating of the culture at 55°C for 19 hours. The crude extract was partially purified using acetone fractionation. Fractionation was carried out at concentrations of acetone at 0-20%, 20-40% and 40-60%. The specific activity was determined by hydrolytic activity of lipase with the substrate of para-nitrophenylpalmitate (pNPP). The result showed that the highest activity of the enzyme is 0.0971 U/mg protein from the fraction of 0-20%. Lipase from isolate AL89 showed optimum activity at 55°C and pH 9. In addition the enzyme prefers para-nitrophenyl laurate (pNPL) as substrate. Using zymography analysis showed that the active protein at the size of 70 kDa. All the data suggested the enzyme is thermo and alkali-tolerant lipase