PULLULANASE
PULLULANASE structure
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Common Name | PULLULANASE | ||
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| CAS Number | 9075-68-7 | Molecular Weight | N/A | |
| Density | 1.25 g/mL at 25 °C(lit.) | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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Gene cloning and enzymatic characterization of alkali-tolerant type I pullulanase from Exiguobacterium acetylicum.
Lett. Appl. Microbiol. 60(1) , 52-9, (2015) A pullulanase gene (Pul3YH5) of 2568 bp, which encodes a protein containing 855 amino acid residues, was cloned from the alkaliphilic bacterium Exiguobacterium acetylicum YH5. The pullulanase (Pul3YH5) contains the YNWGYDP motif of type I pullulanase as well ... |
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Carrier free co-immobilization of alpha amylase, glucoamylase and pullulanase as combined cross-linked enzyme aggregates (combi-CLEAs): a tri-enzyme biocatalyst with one pot starch hydrolytic activity.
Bioresour. Technol. 147 , 269-75, (2013) A tri-enzyme biocatalyst "combi-CLEAs" with starch hydrolytic activity was prepared from commercially available alpha amylase, glucoamylase and pullulanase preparations by aggregating enzymes with ammonium sulphate followed by cross-linking formed aggregates ... |
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Properties of retrograded and acetylated starch produced via starch extrusion or starch hydrolysis with pullulanase.
Carbohydr. Polym. 97(2) , 551-7, (2013) The aim of the present study was to determine the impact of serial modifications of starch, including firstly starch extrusion or hydrolysis with pullulanase, followed by retrogradation (through freezing and defrosting of pastes) and acetylation (under indust... |
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Tumebacillus flagellatus sp. nov., an α-amylase/pullulanase-producing bacterium isolated from cassava wastewater.
Int. J. Syst. Evol. Microbiol. 63(Pt 9) , 3138-42, (2013) A novel α-amylase/pullulanase-producing bacterium, designated strain GST4(T), was isolated from samples collected from the wastewater of a cassava starch factory in Nanning, Guangxi Autonomous Region, southern China. Cells of strain GST4(T) were rod-shaped ba... |
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Effect of C-terminal truncation on enzyme properties of recombinant amylopullulanase from Thermoanaerobacter pseudoethanolicus.
Extremophiles 16(3) , 395-403, (2012) The smallest and enzymatically active molecule, TetApuQ818, was localized within the C-terminal Q818 amino acid residue after serial C-terminal truncation analysis of the recombinant amylopullulanase molecule (TetApuM955) from Thermoanaerobacter pseudoethanol... |
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Structure and properties of maize starch processed with a combination of α-amylase and pullulanase.
Int. J. Biol. Macromol. 52 , 38-44, (2013) The dissolution and digestion characteristics of maize starch processed with a combination of α-amylase and pullulanase (ERS) were investigated. The results were compared with those of high pressure-processed RS (HRS) and regular maize starch. The ERS exhibit... |
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Investigation of the interactions between the hydrophobic cavities of cyclodextrins and pullulanase.
Molecules 16(4) , 3010-7, (2011) The effects of cyclodextrins and derivatives on the activity and structure of pullulanase were investigated in this study. Our results showed that cyclodextrins and derivatives decreased the activity of pullulanase. This decrease was attributed to the interac... |
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Association of HvLDI with limit dextrinase activity and malt quality in barley.
Biotechnol. Lett. 35(4) , 639-45, (2013) Limit dextrinase (LD) is a unique de-branching enzyme involved in starch mobilization of barley grains during malting, and closely related to malt quality. Genotypic variation of LD activity is controlled by genetic factors and also affected by environmental ... |
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Estimation of pullulan by hydrolysis with pullulanase.
Biotechnol. Lett. 32(8) , 1143-5, (2010) A novel method for the estimation of pullulan was developed in which pullulan was hydrolysed by pullulanase. The hydrolysed product was mainly maltotriose and was determined colorimetrically using 3,5-dimethylsalicylic acid. This gave good linearity with resp... |
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An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains.
J. Basic Microbiol. 53(3) , 231-9, (2013) Thermostable amylopullulanase (TAPU) is valuable in starch saccharification industry for its capability to catalyze both α-1,4 and α-1,6 glucosidic bonds under the industrial starch liquefication condition. The majority of TAPUs belong to glycoside hydrolase ... |