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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 02552naa a2200313 4500 | |
| 001 | oai:DiVA.org:ltu-8371 | |
| 003 | SwePub | |
| 008 | 160929s1995 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:ltu:diva-83712 URI |
| 024 | 7 | a https://doi.org/10.1006/abbi.1995.10572 DOI |
| 040 | a (SwePub)ltu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Christakopoulos, Paul4 aut |
| 245 | 1 0 | a Purification and characterization of a less randomly acting endo-1,4-beta-D-glucanase from the culture filtrates of Fusarium oxysporum |
| 264 | 1 | b Elsevier BV,c 1995 |
| 338 | a print2 rdacarrier | |
| 500 | a Upprättat; 1995; 20130220 (ysko) | |
| 520 | a An extracellular endo-1,4-β-D-glucanase from Fusarium oxysporum was purified by affinity chromatography and gel filtration. The enzyme purified in this way was homogeneous when judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing-polyacrylamide gel electrophoresis. The protein corresponded to a molecular mass and pI value of 41.7 kDa and 6.4, respectively. It was optimally active at pH 4.5 and at 55°C. The enzyme hydrolyzed carboxymethylcellulose (CMC) and unsubstituted and substituted cello-oligosaccharides but was inactive on Avicel, filter paper, xylan, cellobiose, p-nitrophenyl-β-D-glucoside, and p-nitrophenyl-β-D-xyloside. However, the enzyme effected only a small change in viscosity of CMC per unit increase of reducing sugar. When cellotriose, cellotetraose, and cellopentaose were used as substrates, the enzyme released mainly cellobiose. Use of 4-methylumbelliferyl cello-oligosaccharides and the determination of bond cleavage frequency revealed that the enzyme preferentially hydrolyzed the glycosidic bond adjacent to 4-methylumbelliferone. Thus, the purified enzyme appeared to be a less randomly acting endoglucanase. | |
| 700 | 1 | a Kekos, D.u National Technical University of Athens4 aut |
| 700 | 1 | a Macris, B.J.u National Technical University of Athens4 aut |
| 700 | 1 | a Claeyssens, M.u University of Ghent4 aut |
| 700 | 1 | a Bhat, M.K.u Institute of Food Research, Reading4 aut |
| 710 | 2 | a National Technical University of Athensb University of Ghent4 org |
| 773 | 0 | t Archives of Biochemistry and Biophysicsd : Elsevier BVg 316:1, s. 428-433q 316:1<428-433x 0003-9861x 1096-0384 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:ltu:diva-8371 |
| 856 | 4 8 | u https://doi.org/10.1006/abbi.1995.1057 |
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