Production and biochemical characterization of Sclerotinia sclerotiorum alpha-amylase ScAmy(1): Assay in starch liquefaction - Université de Limoges Accéder directement au contenu
Article Dans Une Revue Journal of Food Biochemistry Année : 2008

Production and biochemical characterization of Sclerotinia sclerotiorum alpha-amylase ScAmy(1): Assay in starch liquefaction

Résumé

Among the lytic enzymes secreted by the phytopathogen fungus Sclerotinia sclerotiorum, a starch-degrading activity has been isolated and characterized. Two extracellular α-amylases were produced in culture medium in presence of oats flour as carbons sources. An endoamylase named ScAmy1 was purified to homogeneity by ammonium sulfate precipitation, phosphocellulose and cation exchange high performance liquid chromatographies. Molecular mass of purified ScAmy1 was estimated as 54 kDa. Amylase exhibits maximal activity at pH 5 to 6 and at temperature 60C. ScAmy1 was stable in a pH range of (5-11) and at 50C. Initial activity was still conserved 40%, after heating at 60C during 30 min. In addition, Ca2+activate and stabilize the enzyme. Starch end products were determined as low molecular oligoglucanes, the liquefying power of ScAmy1 was also tested with the Amylograph Brabender, results suggest a suitable application of ScAmy1 in several industrial process.

Domaines

Chimie organique

Dates et versions

hal-00687071 , version 1 (12-04-2012)

Identifiants

Citer

Khedher Ben Abdelmalek, Philippe Bressollier, María Camino Urdaci, Ferid Limam, M.Nejib Marzouki. Production and biochemical characterization of Sclerotinia sclerotiorum alpha-amylase ScAmy(1): Assay in starch liquefaction. Journal of Food Biochemistry, 2008, 105 (5), pp.521-528. ⟨10.1111/j.1745-4514.2008.00193.x⟩. ⟨hal-00687071⟩
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