specific detection of pullulanase type i in polyacrylamide

specific detection of pullulanase type i in polyacrylamide

Specific detection of pullulanase type I in polyacrylamide

The specific detection is based on the fact that when pullulanase type I hydrolyzes the 伪-1,6-glycosidic bonds in soluble starch increased amounts of 伪-1,4-linked 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.

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detection of pullulanase in polyacrylamide gels using

Detection of pullulanase in polyacrylamide gels using

Detection of pullulanase in polyacrylamide gels using pullulan-reactive red agar plates. Yang SS, Coleman RD. After electrophoresis, active pullulanase bands in acrylamide gels have been detected by overlaying and then incubating the gel on a replica gel containing 2.5% pullulan-reactive red conjugate and 2.1% agar.

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detection of pullulanase in polyacrylamide gels using

Detection of pullulanase in polyacrylamide gels using

The polyacrylamide gel was soaked twice in fresh 25% isopropanol and 50 mm acetate buffer (pH 5) for 10 min. The gel was then immersed in fresh acetate buffer without iso FiG. 1. Zymogram detection of pullulanase protein and activity. Carbohydrases were electrophoresed on a 7.5% polyacrylamide gel (pH 8.9). The gel was divided into halves.

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(pdf) enzyme electrophoresis in shrimps by polyacrylamide gel

(PDF) Enzyme Electrophoresis in Shrimps by Polyacrylamide Gel

The specific detection is based on the fact that when pullulanase type I hydrolyzes the 伪-1,6-glycosidic bonds in soluble starch increased amounts of 伪-1,4-linked amylose is formed which yields

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fems microbiology letters | vol 116, issue 3, pages 245-368

FEMS Microbiology Letters | Vol 116, Issue 3, Pages 245-368

select article Specific detection of pullulanase type I in polyacrylamide gels. Specific detection of pullulanase type I in polyacrylamide gels. Cheorl-Ho Kim.

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mutational analysis of the pullulanase-type debranching

Mutational Analysis of the Pullulanase-Type Debranching

The specific function of pullulanase-type DBE in the isoamylase-compromised background is not yet known. Both direct and indirect functions are consistent with the data presented here, including preamylopectin processing, a role in the metabolism of maltooligosaccharides, and involvement in starch granule initiation.

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purification and biochemical characterization of pullulanase

Purification and biochemical characterization of pullulanase

A thermostable pullulanase (pullulan 6-glucanohydrolase, EC 3.2.1.41) has been purified to homogeneity from Thermus caldophilus GK-24 by Chromatographic methods, including gel-filtration and ion-exchange chromatography. The specific activity of the enzyme was increased 431-fold with a recovery of 13.2%.

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purification of pullulanase from aureobasidium pullulan s

Purification of pullulanase from Aureobasidium pullulan s

The specific detection is based on the fact that when pullulanase type I hydrolyzes the 伪-1,6-glycosidic bonds in soluble starch increased amounts of 伪-1,4-linked amylose is formed which yields

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