Malakar ramdas (6 risultati)
Pullulanase: A Potantial Enzyme: Effect Of Media Composition And Culture Condition On Pullulanase Enzyme From Extremophile Bacterial Species
Malakar, Ramdas; Malviya, S. N.; Yadav, Mahaveer; Malakar, Ramdas; Malviya, S. N.; Yadav, Mahaveer
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Da: Revaluation Books, Exeter, Regno UnitoRevaluation Books
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Paperback. Condizione: Brand New. 116 pages. 8.66x5.91x0.27 inches. In Stock.
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Da: preigu, Osnabrück, Germaniapreigu
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Taschenbuch. Condizione: Neu. Pullulanase: A Potantial Enzyme | Effect of Media Composition and Culture Condition on Pullulanase Enzyme from Extremophile Bacterial Species | Ramdas Malakar (u. a.) | Taschenbuch | 116 S. | Englisch | 2018 | LAP LAMBERT Academic Publishing | EAN 9783659382260 | Verantwortliche Person für die EU: p…reigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.
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Da: Mispah books, Redhill, SURRE, Regno UnitoMispah books
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paperback. Condizione: New. NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
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Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermaniaBuchWeltWeit Ludwig Meier e.K.
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Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The roles of enzymes in many processes have been known for long time. Their existence was associated with the history of ancient Greece where they were using enzyme from microorganism in baking, brewing, alcohol production, cheese…making etc. With better knowledge and purification of enzyme a number of applications has increased many folds, and with the availability of the enzyme a number of new possibilities for industrial process have immerged. Pullulanase is one such industrially useful enzyme used in the starch processing industries. Pullulanase belongs to -amylase class of enzymes which is an extracellular carbohydrase which was first discovered by Bender and Wallenfels in 1961 from mesophilic organism Klebsiella pneumoniae (formerly known as Aerobactor aerogenes or Klebsiella aerogenes). Pullulanase are also called de-branching enzyme which hydrolyze the extracellular yeast, polysaccharide and pullulan. It converts pullulan into the trisaccharides, maltotriose. It consists of repeating units of -maltotriose joined 'head to tail' by 1,6-bonds. Pullulanase specifically attack on -1,6-glycosidic linkage and it also attacks on -1,4-glycosidic linkage with other residues. 116 pp. Englisch.
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Da: moluna, Greven, Germaniamoluna
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Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Malakar RamdasI am R. D. Malakar Research Scholar of School of Biotechnology Rajiv Gandhi Proudyogiki Vishwavidyalaya Bhopal Madhya Pradesh India. I have a Bachelor and Master Degree in life Science an…d I have also completedthe Maste.
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Da: buchversandmimpf2000, Emtmannsberg, BAYE, Germaniabuchversandmimpf2000
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Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The roles of enzymes in many processes have been known for long time. Their existence was associated with the history of ancient Greece where they were using enzyme from microorganism in baking, brewing, alcohol production, cheese maki…ng etc. With better knowledge and purification of enzyme a number of applications has increased many folds, and with the availability of the enzyme a number of new possibilities for industrial process have immerged. Pullulanase is one such industrially useful enzyme used in the starch processing industries. Pullulanase belongs to ¿-amylase class of enzymes which is an extracellular carbohydrase which was first discovered by Bender and Wallenfels in 1961 from mesophilic organism Klebsiella pneumoniae (formerly known as Aerobactor aerogenes or Klebsiella aerogenes). Pullulanase are also called de-branching enzyme which hydrolyze the extracellular yeast, polysaccharide and pullulan. It converts pullulan into the trisaccharides, maltotriose. It consists of repeating units of ¿-maltotriose joined 'head to tail' by 1,6-bonds. Pullulanase specifically attack on ¿-1,6-glycosidic linkage and it also attacks on ¿-1,4-glycosidic linkage with other residues.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 116 pp. Englisch.
