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Title of Journal: FEMS Microbiol Lett

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Abbravation: FEMS Microbiology Letters

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Narnia

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0378-1097

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Specific detection of pullulanase type I in polyac

Authors: Kim CheorlHo
Publish Date: 1994/03/01
Volume: 116, Issue: 3, Pages: 327-331
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Abstract

A specific detection of pullulanase type I which hydrolyzes the α16glycosidic linkages on pullulan and starch was developed using impregnation of gels with soluble starch and staining for amylose with iodine It was a simple and highly sensitive zymogram method capable of detecting as little as 0001 unit of pullulanase type I activity in polyacrylamide gels after electrophoresis After fractionation of crude enzyme using DEAE ion exchange chromatography to avoid possible comigration of amylolytic enzymes which disturb the interaction between amylose and iodine the high and critical sensitivity of the detection was achieved The specific detection is based on the fact that when pullulanase type I hydrolyzes the α16glycosidic bonds in soluble starch increased amounts of α14linked amylose is formed which yields more intensely blue colored conjugate with iodine Thus blue bands on the lighter background signal the presence of pullulanase type I In contrast amylolytic enzymes give ‘white’ bands on the lightly stained background because they remove amylose This procedure is effective in enzyme screening to distinguish debranching enzyme pullulanase type I from other pullulandegrading enzymes

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References

citation title=Purification and properties of a thermostable pullulanase from Clostridium thermosulforogenes EM1 which hydrolyzes both α16 and α14glycosidic linkages citation author=Spreinat A citation author=Antranikian G citation journal title=Appl Microbiol Biotechnol citation year=1990 citation volume=33 citation pages=511518

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  11. Characterization of glucoamylase from Aspergillus terreus 4
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  14. Monoxenic cultivation of the anaerobic amoeboflagellate Psalteriomonas lanterna and isolation of the methanogenic endosymbiont
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