http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
β-Glucosidase Recovery from a Solid-State Fermentation System by Aspergillus niger
M. Subhosh Chandra(수보쉬 찬드라),B. Rajasekhar Reddy(라자세카 레디),Yong Lark Choi(최용락) 한국생명과학회 2010 생명과학회지 Vol.20 No.7
밀기울 발효에서 효소회수의 모델로 Aspergillus niger를 고체상태로 발효시켜 조사하였다. 발효시킨 밀기울에서 증류수로 효소추출 효율은 초산 완충액, 구연산 완충액, 구연산-인산 완충액 및 5% 메탄올 처리보다 높았다. 따라서, 추출 용매로 증류수를 이용하여 최적 조건을 상세히 검토하였다. 최적 조건은 고체와 액체 용매를 1:5의 비율로 증류수로서 세 번 세척하였을 때에 최대 회수율을 0.025 U/g으로 확보하였다. Investigations were carried out on a β-glucosidase produced by Aspergillus niger under solid-state fermentation conditions as a model of enzyme recovery from fermented wheat bran. The leaching efficiency of distilled water to recover the enzyme from the fermented bran was higher than acetate buffer, citrate buffer, citrate-phosphate buffer and 5% methanol; thus, the conditions were further optimized with distilled water as the extracting agent. After fermented bran was washed three times with distilled water for 1.5 hr each under shaking conditions at 1:5 solid to solvent ratio, a maximum recovery of 0.025 U/g of wheat bran was obtained.
Production of Cellulolytic Enzymes by Aspergillus niger on Solid and Submerged State Fermentation
M. Subhosh Chandra(수보쉬 찬드라),B. Rajasekhar Reddy(라자세카르 레디),Yong Lark Choi(최용락) 한국생명과학회 2008 생명과학회지 Vol.18 No.8
Aspergillus niger가 액체발효(SF) 와 고체발효의 시험 규모 조건에서의 셀루로오스계 효소의 생산을 비교하였다. 액체배지는 0.5% 셀루로오스가 함유된 Czapek Dox를 사용하였고, 고체 지지체로 사용한 쌀겨는 셀루로오스로 적시고 SSF 발효를 위하여 Czapek Dox 배지를 첨가하였다. CMCase, 여지 paperase 그리고 β-Glucosidase의 생산을 경시적으로 측정하였다. SSF 배양에서의 3일간의 효소 생산량은 SF 에서의 7일간 배양과 같았다. 따라서 SSF 조건이 SF 배양 조건보다 많은 효소를 생산함을 알 수 있었다. SSF 조건에서 FPase, CMCase 및 β-glucosidase의 최대 활성은 0.40, 0.62 및 0.013 U/ml 였으나, SF 조건에서는 0.13, 0.06 및 0.0013 U/ml의 활성을 나타내었다. 결론적으로 Aspergillus niger에 의해 생산되는 셀루로오스계 효소의 생산을 위해서는 SSF 발효 조건의 선택이 유리하다는 것을 알 수 있었다. Microbial production of cellulolytic enzymes by Aspergillus niger in solid state fermentation (SSF) and submerged state fermentation (SF) in laboratory scale was compared. Czapek Dox liquid broth amended with cellulose (0.5%) was used for cultivation in SF, whereas rice bran was used as a solid support, moistened with cellulose, amended Czapek Dox broth for growth in SSF. The production of Carboxymethyl cellulase, Filter paperase and β-Glucosidase was monitored at regular intervals. The peak production of the enzymes occurred within 3 days of incubation in SSF as against ≥ 7 days in SF. SSF gave higher yields of enzymes in comparison to SF. Maximum titres of 0.40, 0.62 and 0.013 U/ml in respect of FPase, CMCase and β-glucosidase in SSF were recovered as against 0.13, 0.06 and 0.0013 U/ml in SF respectively, at their respective peak time intervals. Hence, SSF appeared to be a better choice for production of cellulolytic enzymes by Aspergillus niger.
( Muni Rammannagari Subhosh Chandra ),( Yong Suk Lee ),( In Hye Park ),( Yi Zhou ),( Keun Ki Kim ),( Yong Lark Choi ) 한국응용생명화학회 2011 Applied Biological Chemistry (Appl Biol Chem) Vol.54 No.3
Paenibacillus sp. DZ3, newly isolated from Konjack field, produced β-mannanase (900 U/mL) when grown on glucomannan as a carbon source. β-Mannanase was purified 34-fold to homogeneity resulting in final recovery of 15% and specificity of 169 U/mg protein. The molecular mass was approximately 39 kDa as estimated by sodiumdodecylsulfate-polyacrylamide gel electrophoresis. Active band was observed as clear colourless area on zymogram. The optimal temperature and pH for mannanase activity was 60˚C and pH 5.0, respectively. The activity was stable up to 60˚C at pH 5.0 and remained stable from pH 5.0-7.0. Mannanase was highly specific towards glucomannan and galactomannan, whereas exhibited low activity towards mushroom powder. The Michaelis constant (Km) and maximum velocity (Vmax) for glucomannan substrate were 1.05 mg/mL and 714 U/mg, respectively. These results indicate the enzyme is attractive for industrial applications.
G. Satheesh Kumar,M. Subhosh Chandra,M. Sumanth,A. Vishnupriya,B. Rajasekhar Reddy,Yong-Lark Choi 한국응용생명화학회 2009 Journal of Applied Biological Chemistry (J. Appl. Vol.52 No.1
Newly isolated strains Bacillus sp. FME 1 and FME 2 were evaluated for the cellulolytic enzymes production during submerged fermentation (SmF) of different substrates including rice husk, Whatman filter paper and cellulose powder CF 11. Extracellular enzyme assays for CMCase, FPase and β-glucosidase were examined up to 8 days of submerged fermentation. Among the three substrates, rice husk was the most suitable substrate for higher production of cellulolytic enzymes. Maximum titers of 100, 45, and 3.5 U/mL in respect of CMCase, FPase and β-glucosidase in Bacillus sp. FME 2 were recovered as against 45, 12, and 0.39 U/mL in Bacillus sp. FME 1 respectively, at their respective peak time intervals. Bacillus sp. FME 2 was found to produce higher cellulolytic enzyme activities than Bacillus sp. FME 1.
Enhanced Production and Partial Purification of Glucoamylase from Mutated Bacillus sp. FME
Kumar, Gudi Satheesh,Chandra, Muni Ramanna Gari Subhosh,Sujana, Yakasiri Nagasai,Reddy, Bontha Rajasekhar,Choi, Yong-Lark The Korean Society for Applied Biological Chemistr 2009 Applied Biological Chemistry (Appl Biol Chem) Vol.52 No.5
In this study, a potent newly-isolated glucoamylase producing actively growing cells of Bacillus sp. FME was subjected to UV irradiation and ethidium bromide (EtBr) mutagenesis. The promising colonies were further screened for glucoamylase production via plate assays and submerged enzyme production at the flask level. Amongst all of the tested colonies, the best mutant, Bacillus sp. FME 2, selected from UV irradiation (20 min) and EtBr (1 mg/mL), was shown to be the most promising. The yield of glucoamylase generated by the mutant strain was approximately 3.0 fold and 1397 U/mL with an incubation period of 24 h, which was larger than the yield generated by the wild-type strain. The glucoamylase was partially purified using ammonium sulphate precipitation followed by gel exclusion chromatography. The enzyme was partially purified 3.0-fold to homogeneity with a final recovery of 66% and a specific activity of 1145 U/mg protein for the mutant strain. The molecular mass was approximately 67.1 kDa, as determined by SDS-PAGE. The active band was observed as a clear colorless area on zymogram analysis, which indicated an absence of glucoamylase isoforms. The results of thin-layer chromatography identified this enzyme as a glucoamylase.