Isolation of α-amylase on crosslinked starch

Starch and Microbial α-Amylases: From Concepts to Biotechnological Applications

“…The most commonly used techniques are usually affinity chromatography, ion exchange, and/or gel filtration. Cross-linked starch or starch derivatives are useful affinity adsorbents for the isolation of bacterial -amylases (Somers et al, 1995). Primarini & Ohta (2000) isolated and separated two pure -amylases from Streptomyces sp.…”

Adsorptive Properties of the Preparation Material from the Skin of Corn Stalk for Enzyme Immobilization

“…At first preparation technology of the biocatalysts by surface adsorption was used during the immobilization processes. The starch and starch derivatives may be used adsorbents [5][6][7][8] because it has biological and chemical properties such as hydrophilicity, biodegradability, polyfunctionality, high chemical reactivity, and adsorption capacities. However, the world-wide food-supplies crisis and the hydrophilic nature of starch are major constraint, which seriously limits the development of adsorption materials.…”

Phage display selects for amylases with improved low pH starch-binding

“…Therefore we decided to study if the C-terminal domain of the B. licheniformis a-amylase is indeed involved in starchbinding and to explore the possibility to develop a phage display selection method for a-amylase mutants which have altered starch-binding. The starch-binding property was, without relating this property to a specific part of the protein molecule, already used to develop a large-scale purification procedure, which involves affinity chromatography to raw starch or cross-linked starch (Weber et al, 1976;Rozie et al, 1991;Satoh et al, 1993;Somers et al, 1995). Interestingly at pH 4.5 the enzyme shows a reasonable hydrolytic activity on the small substrate heptamaltose, whereas the activity on polymeric starch is zero.…”