Purification and some properties of an alpha-amylase glucoamylase fusion protein from Saccharomyces cerevisiae
A fusion gene containing the Bacillus subtilis alpha -amylase gene and Aspergillus awamori glucoamylase cDNA was expressed in Saccharomyces cerevisiae. The resulting bifunctional fusion protein having both alpha -amylase and glucoamylase activities secreted into the culture medium was purified to ap...
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| Veröffentlicht in: | World journal of microbiology & biotechnology 1999-10, Vol.15 (5), p.561-564 |
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| container_end_page | 564 |
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| container_issue | 5 |
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| container_title | World journal of microbiology & biotechnology |
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| creator | Moraes, L.M.P. de Astolfi Filho, S Ulhoa, C.J |
| description | A fusion gene containing the Bacillus subtilis alpha -amylase gene and Aspergillus awamori glucoamylase cDNA was expressed in Saccharomyces cerevisiae. The resulting bifunctional fusion protein having both alpha -amylase and glucoamylase activities secreted into the culture medium was purified to apparent homogeneity by affinity chromatography and gel filtration on Sephadex G-100. The enzyme had an apparent molecular mass of 150 kDa and showed an optimum pH and temperature of 6.0 and 60 degree C, respectively. The main hydrolysis products from soluble starch were glucose and maltose. |
| doi_str_mv | 10.1023/A:1008961015119 |
| format | Article |
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The resulting bifunctional fusion protein having both alpha -amylase and glucoamylase activities secreted into the culture medium was purified to apparent homogeneity by affinity chromatography and gel filtration on Sephadex G-100. The enzyme had an apparent molecular mass of 150 kDa and showed an optimum pH and temperature of 6.0 and 60 degree C, respectively. The main hydrolysis products from soluble starch were glucose and maltose.</description><identifier>ISSN: 0959-3993</identifier><identifier>EISSN: 1573-0972</identifier><identifier>DOI: 10.1023/A:1008961015119</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Aspergillus awamori ; Bacillus subtilis ; Biological and medical sciences ; Biotechnology ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; glucan 1,4-alpha-glucosidase ; Methods. Procedures. 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The resulting bifunctional fusion protein having both alpha -amylase and glucoamylase activities secreted into the culture medium was purified to apparent homogeneity by affinity chromatography and gel filtration on Sephadex G-100. The enzyme had an apparent molecular mass of 150 kDa and showed an optimum pH and temperature of 6.0 and 60 degree C, respectively. The main hydrolysis products from soluble starch were glucose and maltose.</description><subject>Aspergillus awamori</subject><subject>Bacillus subtilis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Enzyme engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glucan 1,4-alpha-glucosidase</subject><subject>Methods. Procedures. 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Psychology</topic><topic>glucan 1,4-alpha-glucosidase</topic><topic>Methods. Procedures. 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The resulting bifunctional fusion protein having both alpha -amylase and glucoamylase activities secreted into the culture medium was purified to apparent homogeneity by affinity chromatography and gel filtration on Sephadex G-100. The enzyme had an apparent molecular mass of 150 kDa and showed an optimum pH and temperature of 6.0 and 60 degree C, respectively. The main hydrolysis products from soluble starch were glucose and maltose.</abstract><cop>Dordrecht</cop><pub>Springer</pub><doi>10.1023/A:1008961015119</doi><tpages>4</tpages></addata></record> |
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| ispartof | World journal of microbiology & biotechnology, 1999-10, Vol.15 (5), p.561-564 |
| issn | 0959-3993 1573-0972 |
| language | eng |
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| source | SpringerLink Journals |
| subjects | Aspergillus awamori Bacillus subtilis Biological and medical sciences Biotechnology Enzyme engineering Fundamental and applied biological sciences. Psychology glucan 1,4-alpha-glucosidase Methods. Procedures. Technologies Miscellaneous Sephadex G-100 |
| title | Purification and some properties of an alpha-amylase glucoamylase fusion protein from Saccharomyces cerevisiae |
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