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DC Field | Value | Language |
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dc.contributor.author | Mukherjee, Abhishek | - |
dc.contributor.author | Ghosh, Anil K. | - |
dc.contributor.author | Sengupta, Subhabrata | - |
dc.date.accessioned | 2019-05-24T05:25:49Z | - |
dc.date.available | 2019-05-24T05:25:49Z | - |
dc.date.issued | 2010-12-10 | - |
dc.identifier.issn | 0008-6215 | - |
dc.identifier.uri | http://172.16.0.4:8085/heritage/handle/123456789/3163 | - |
dc.description.abstract | A 43 kDa a-amylase was purified from Tinospora cordifolia by glycogen precipitation, ammonium sulfate precipitation, gel filtration chromatography, and HPGPLC. The enzyme was optimally active in pH 6.0 at 60 C and had specific activity of 546.2 U/mg of protein. Activity was stable in the pH range of 4–7 and at temperatures up to 60 C. PCMB, iodoacetic acid, iodoacetamide, DTNB, and heavy metal ions Hg2+ > Ag+ > Cd2+ inhibited enzyme activity while Ca2+ improved both activity and thermostability. The enzyme was a thiol amylase (3 SH group/mole) and DTNB inhibition of activity was released by cysteine. N-terminal sequence of the enzyme had poor similarity (12–24%) with those of plant and microbial amylases. The enzyme was equally active on soluble starch and amylopectin and released maltose as the major end product. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsvier | en_US |
dc.relation.ispartofseries | Vol. 345;Issue 18 | - |
dc.subject | Tinospora cordifolia | en_US |
dc.subject | Amylase | en_US |
dc.subject | Thiol amylase | en_US |
dc.subject | Amylopectin | en_US |
dc.subject | Glycogen | en_US |
dc.subject | Cereal flour | en_US |
dc.title | Purification and characterization of a thiol amylase over produced by a non-cereal non-leguminous plant, tinospora cordifolia | en_US |
dc.title.alternative | (In) Carbohydrate Research | en_US |
dc.type | Article | en_US |
Appears in Collections: | Biotechnology (Publications) |
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File | Description | Size | Format | |
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CAR5546.pdf | 414.88 kB | Adobe PDF | View/Open |
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