http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Anamika Sharma,Vikrant Nain,Rameshwar Tiwari,Surender Singh,Anurup Adak,Pawan Kumar Singh Nain,Lata Nain 한국화학공학회 2017 Korean Journal of Chemical Engineering Vol.34 No.3
The present investigation was aimed towards pretreatment optimization of corncob to maximize cellulose and hemicellulose recovery, followed by substrate selection for holocellulase production using psychrotolerant Aspergillus niger SH3. Dilute alkali pretreatment (1.5% NaOH) resulted in higher recovery of cellulose (59.66%) and hemicellulose (28.34%) from corncob, while corn stover proved to be the best substrate for holocellulase production. Further, saccharification was optimized by Box-Behnken design to select the suitable conditions for maximum sugar release from pretreated corncob. The optimum conditions for maximum sugar release were 8% (w/v) substrate loading, 11 FPU/gds enzyme loading at temperature 38 oC and pH 3.0 which resulted in 114.5% higher sugar yield (912mg/gds of pretreated biomass) as compared with un-optimized conditions (425.35mg/gds). Theoretical yield of 48.8% ethanol was achieved through simultaneous saccharification and fermentation (SSF) using pretreated corncob. This study illustrates the potential of different corn residues as a promising substrate for bioethanol production.
( Sangeeta Pandey ),( Rameshwar Tiwari ),( Surender Singh ),( Lata Nain ),( Anil Kumar Saxena ) 한국미생물 · 생명공학회 2014 Journal of microbiology and biotechnology Vol.24 No.8
A total of 10 cellulase-producing bacteria were isolated from soil samples irrigated with paper and pulp mill effluents. The sequencing of 16S rRNA gene revealed that all isolates belonged to different species of genus Bacillus. Among the different isolates, B. subtilis IARI-SP-1 exhibited a high degree of β-1,4-endoglucanase (2.5 IU/ml), β-1,4-exoglucanase (0.8 IU/ml), and β-glucosidase (0.084 IU/ml) activity, followed by B. amyloliquefaciens IARI-SP-2. CMC was found to be the best carbon source for production of endo/exoglucanase and β-glucosidase. The β-1,4-endoglucanase gene was amplified from all isolates and their deduced amino acid sequences belonged to glycosyl hydrolase family 5. Among the domains of different isolates, the catalytic domains exhibited the highest homology of 93.7%, whereas the regions of signal, leader, linker, and carbohydrate-binding domain indicated low homology (73-74%). These variations in sequence homology are significant and could contribute to the structure and function of the enzyme.
( Kumar Pranaw ),( Surender Singh ),( Debjani Dutta ),( Nirpendra Singh ),( Garima Sharma ),( Sudershan Ganguly ),( Vinay Kalia ),( Lata Nain ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.11
Proteases produced by Xenorhabdus are known to play a significant role in virulence leading to insect mortality. The present study was undertaken to purify and characterize protease from Xenorhabdus indica, an endosymbiont of nematode Steinernema thermophilum, and to decipher its role in insect mortality and its efficacy to control Helicoverpa armigera. A set of 10 strains of Xenorhabdus isolated from different regions of India were screened for protease activity on the basis of zone of clearing on gelatin agar plates. One potent strain of Xenorhabdus indica was selected for the production of protease, and the highest production (1,552 U/ml) was observed at 15-18 h of incubation at 28oC in soya casein digest broth. The extracellular protease was purified from culture supernatant using ammonium sulfate precipitation and ion-exchange chromatography. The enzyme was further characterized by SDS-PAGE and zymography, which confirmed the purity of the protein and its molecular mass was found to be ~52 kDa. Further MALDI-TOF/TOF analysis and effect of metal chelating agent 1,10-phenanthrolin study revealed the nature of the purified protease as a secreted alkaline metalloprotease. The bioefficacy of the purified protease was also tested against cotton bollworm (Helicoverpa armigera) and resulted in 67.9 ± 0.64% mortality within one week. This purified protease has the potential to be developed as a natural insecticidal agent against a broad range of agriculturally important insects.