Pullulanase bacterial

Arnosti, C., and D. J. Repeta. 1994a. Extracellular enzyme activity in anaerobic bacterial cultures Evidence of pullulanase activity among mesophilic marine bacteria. Applied and Environmental Microbiology 60 840-846. 

Lipase (Microbial) Activity for Medium- and Long-Chain Fatty Acids, (S3)105 Lysozyme Activity, (S3)106 Maltogenic Amylase Activity, 804 Milk-Clotting Activity, 805 Pancreatin Activity, 805 Pepsin Activity, 807 Phospholipase A2 Activity, 808 Phytase Activity, 808 Plant Proteolytic Activity, 810 Proteolytic Activity, Bacterial (PC), 811 Proteolytic Activity, Fungal (HUT), 812 Proteolytic Activity, Fungal (SAP), 813 Pullulanase Activity, 814 Trypsin Activity, 814 Enzyme Assays, 786 Enzyme-Hydrolyzed (Source) Protein,... 

The hypothesis that the sugary 1 mutation affects the structural gene for a debranching enzyme is further supported by the isolation of a cDNA of the su 1 gene. However, its deduced amino-acid sequence is similar to a bacterial isoamylase (James et al, 1995) rather than to a pullulanase. 

The plant and bacterial enzymes capable of hydrolyzing pullulan do not have identical specificities. In particular, the plant enzymes have little or no action on glycogen and phytoglycogen under conditions in which they readily hydrolyze amylopectin and its /3-dextrin. To stress this difference (the bacterial enzymes are capable of degrading both glycogen and phytoglycogen), Manners (1997) recommended different nomenclature for bacterial enzymes, to be called pullulanase, and the plant enzymes, to be called limit dextrinases. 

Sources of Bacillus. Since Bacillus had proved to be such a valuable source of industrial enzymes since early this century, much screening for new enzymes concentrated initially on these bacteria (4). The results were not disappointing. The first bacterial p-amylases were discovered in B. polymyxa (5 7), B. cereus (8) and B. megaterium (9,10) and the genus is a rich source of pullulanases (11) with commercial production from B. 

The production of thermostable enzymes, catalyzing reactions at high temperatures, is one of the most attractive features of thermophilic microorganisms. In order to select producers of thermostable hydrolases, different aerobic thermophilic bacterial strains were Isolated from water, soil and organic material samples collected from Bulgarian hot springs environment. Some of the properties of the Isolated strains were a subject of our previous work [1]. The aim of the present paper was to characterize and identify the strain producing thermostable pullulanase as well as to establish the optimum conditions for enzyme production and to study some of the enzyme s properties. 

Pullulanase (EC 3.2.1.41) is a typical bacterial endo-splitting enzyme that hydrolyses the a-l,6-glucosidic bonds of pullulan, amylopectin and their a- and p-limit dextrins. Pullulanase requires that each of the two chains of amylopectin linked by an a-1,6-glucosidic bond contain at least two adjacent a-l,4-linked glucose imits. 

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