Building Resilience and Social-Emotional Competencies in Elementary School Students through a Short-Term Intervention Program Based on the SEE Learning Curriculum.

This study explored the positive effects of a six-week Social-Emotional and Ethical Learning® (SEE Learning) program on resilience and social and emotional competences, adapted for elementary students in Daegu, South Korea, a region strongly affected by the first outbreak of COVID-19. A total of 348 third- and fourth-grade students from 15 elementary schools participated, and the curriculum was tailored, emphasizing key areas such as resilience, attention, kindness, attention training, and compassion. Repeated measures analysis of variance (RMANOVA) tests showed statistically significant improvements between pre- and post-tests in resilience and its subscales, including self-efficacy, tolerance of negative affect, positive support relations, power of control, and spontaneity, as well as in social and emotional competencies, including emotional regulation, social skills, empathy, and social tendencies. Despite a lack of maintenance in all areas, at follow-up, the mean scores for self-efficacy, tolerance of negative affect, and positive support relations, as well as emotional regulation, social skills, empathy, and social tendency, remained higher than pre-test levels, suggesting some lasting benefits. The findings underscore the potential of the SEE Learning program integrated with resilience, mindfulness, compassion, and ethical practices to enhance students' resilience and social and emotional well-being. This study contributes to the growing body of evidence supporting the use of mindfulness and compassion-based SEL programs to mitigate the adverse effects of traumatic events on children's mental health.

Enhanced production of carboxymethylcellulase of a marine microorganism, Bacillus subtilis subsp. subtilis A-53 in a pilot-scaled bioreactor by a recombinant Escherichia coli JM109/A-53 from rice bran.

A gene encoding the carboxymethylcellulase (CMCase) of a marine bacterium, Bacillus subtilis subsp. subtilis A-53, was cloned in Escherichia coli JMB109 and the recombinant strain was named as E. coli JMB109/A-53. The optimal conditions of rice bran, ammonium chloride, and initial pH of the medium for cell growth, extracted by Design Expert Software based on response surface methodology, were 100.0 g/l, 7.5 g/l, and 7.0, respectively, whereas those for production of CMCase were 100.0 g/l, 7.5 g/l, and 8.0. The optimal temperatures for cell growth and the production of CMCase by E. coli JM109/A-53 were found to be and 40 and 35 °C, respectively. The optimal agitation speed and aeration rate of a 7 l bioreactor for cell growth were 400 rpm and 1.5 vvm, whereas those for production of CMCase were 400 rpm and 0.5 vvm. The optimal inner pressure for cell growth was 0.06 MPa, which was the same as that for production of CMCase. The production of CMCase by E. coli JM109/A-53 under optimized conditions was 880.2 U/ml, which was 2.9 times higher than that before optimization. In this study, rice bran and ammonium chloride were developed as carbon and nitrogen source for production of CMCase by a recombinant E. coli JM109/A-53 and the productivity of E. coli JM109/A-53 was 5.9 times higher than that of B. subtilis subp. subtilis A-53.

Purification and characterization of cellulase produced by Bacillus amyoliquefaciens DL-3 utilizing rice hull.

A microorganism hydrolyzing rice hull was isolated from soil and identified as Bacillus amyloliquefaciens by analysis of 16S rDNA and partial sequences of the gyrA gene, and named as B. amyloliquefaciens DL-3. With the analysis of SDS-PAGE, the molecular weight of the purified cellulase was estimated to be 54kDa. The purified cellulase hydrolyzed avicel, caboxymethylcellulose (CMC), cellobiose, beta-glucan and xylan, but not p-Nitrophenyl-beta-D-glucopyranoside (PNPG). Optimum temperature and pH for the CMCase activity of the purified cellulase were found to be 50 degrees C and pH 7.0, respectively. The CMCase activity was inhibited by some metal ions, N-bromosuccinimide and EDTA in the order of Hg(2+)>EDTA>Mn(2+)>N-bromosuccinimide>Ni(2+)>Pb(2+)>Sr(2+)>Co(2+)>K(+). The open reading frame of the cellulase from B. amyloliquefaciens DL-3 was found to encode a protein of 499 amino acids. The deduced amino acid sequence of the cellulase from B. amyloliquefaciens DL-3 showed high identity to cellulases from other Bacillus species, a modular structure containing a catalytic domain of the glycoside hydrolase family 5 (GH5), and a cellulose-binding module type 3 (CBM3).