Defatting improves the hydrolysis of granular starch using a mixture of fungal amylolytic enzymes

The effect of compositions of bitter cassava (Manihot glaziovii) and gadung (Dioscorea hispida Dennst) starches on reducing sugar during hydrolysis using granular starch hydrolyzing enzyme (GSHE) was studied. All hydrolyses were conducted at concentration of substrate was 200 g.L-1, while concentration of enzyme was 1.5 % (w/w), during of hydrolysis time 24 h, at 30°C. Mass compositition of bitter cassava and gadung starches were 9:1 to 1:9 The increase gadung starch compositions will decrease the reducing sugar. The optimum condition of the process using concentration of substrate 200 g.L-1 with compositions of bitter cassava and gadung starches was 9:1 at 18 h. It was found that reducing sugar was 50.20 g.L-1. The concentration of reducing sugar mainly depend on starch content on bitter cassava, it is much bigger than the gadung starch.

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Bacillus stearothermophilus Neopullulanase Selective Hydrolysis of Amylose to Maltose in the Presence of Amylopectin

Applied and Environmental Microbiology ◽

10.1128/aem.68.4.1658-1664.2002 ◽

2002 ◽

Vol 68 (4) ◽

pp. 1658-1664 ◽

Cited By ~ 32

Author(s):

Hiroshi Kamasaka ◽

Kazuhisa Sugimoto ◽

Hiroki Takata ◽

Takahisa Nishimura ◽

Takashi Kuriki

Keyword(s):

Substrate Specificity ◽

Bacillus Licheniformis ◽

Bacillus Megaterium ◽

Bacillus Stearothermophilus ◽

Main Product ◽

Selective Hydrolysis ◽

Amylolytic Enzymes ◽

Order Of Magnitude ◽

Maltogenic Amylase ◽

Hydrolysis Of

ABSTRACT The specificity of Bacillus stearothermophilus TRS40 neopullulanase toward amylose and amylopectin was analyzed. Although this neopullulanase completely hydrolyzed amylose to produce maltose as the main product, it scarcely hydrolyzed amylopectin. The molecular mass of amylopectin was decreased by only one order of magnitude, from approximately 108 to 107 Da. Furthermore, this neopullulanase selectively hydrolyzed amylose when starch was used as a substrate. This phenomenon, efficient hydrolysis of amylose but not amylopectin, was also observed with cyclomaltodextrinase from alkaliphilic Bacillus sp. strain A2-5a and maltogenic amylase from Bacillus licheniformis ATCC 27811. These three enzymes hydrolyzed cyclomaltodextrins and amylose much faster than pullulan. Other amylolytic enzymes, such as bacterial saccharifying α-amylase, bacterial liquefying α-amylase, β-amylase, and neopullulanase from Bacillus megaterium, did not exhibit this distinct substrate specificity at all, i.e., the preference of amylose to amylopectin.

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Hydrolysis of amylopectin by amylolytic enzymes: level of inner chain attack as an important analytical differentiation criterion

Carbohydrate Research ◽

10.1016/j.carres.2009.11.011 ◽

2010 ◽

Vol 345 (3) ◽

pp. 397-401 ◽

Cited By ~ 25

Author(s):

Hans Goesaert ◽

Annabel Bijttebier ◽

Jan A. Delcour

Keyword(s):

Amylolytic Enzymes ◽

Hydrolysis Of

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Inhibitory Effects of Cyanide on the Activity of Granular Starch Hydrolyzing Enzyme (GSHE) during Hydrolysis of Cassava (Manihot Esculenta Crantz) Starch

Periodica Polytechnica Chemical Engineering ◽

10.3311/ppch.12006 ◽

2018 ◽

Vol 63 (1) ◽

pp. 11-17

Author(s):

Hargono Hargono ◽

Andri Cahyo Kumoro ◽

Bakti Jos

Keyword(s):

Manihot Esculenta ◽

Maximum Velocity ◽

Cassava Starch ◽

Inhibitory Effects ◽

Manihot Esculenta Crantz ◽

Km Value ◽

Hydrolysis Of ◽

Reducing Sugar Concentration ◽

Granular Starch ◽

Burk Plot

The kinetics and inhibitory effects of cyanide on the granular starch hydrolyzing enzyme (GSHE) activity during hydrolysis of cassava (Manihot esculenta Crantz) starch at low temperature were studied. The substrates included native cassava starch at various concentrations (100-400 g/L) and native cassava starches with added cyanide at various concentrations (50-150 mg/kg), while the concentration of enzyme was 1.5% (w/w). A decrease in reducing sugar concentration during hydrolysis of cassava starch indicated that the cyanide reduced the enzyme activity. Lineweaver-Burk plot of Michaelis-Menten equation was used to study the inhibition kinetics. The maximum velocity (Vmax) value was higher for native cassava starch than that of native cassava starch with added cyanides. The presence of cyanide was found to reduce the Vmax values. No significant different of the saturation constant (Km) value between native cassava starch and native cassava starch with added cyanides was observed. Based on the inhibition type analysis, the effect of cyanide in the cassava starch can be classified as a noncompetitive inhibition, with the Ki value of 0.33 mg/L.

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Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin population

Carbohydrate Research ◽

10.1016/j.carres.2009.11.010 ◽

2010 ◽

Vol 345 (2) ◽

pp. 235-242 ◽

Cited By ~ 33

Author(s):

Annabel Bijttebier ◽

Hans Goesaert ◽

Jan A. Delcour

Keyword(s):

Structural Analysis ◽

Amylolytic Enzymes ◽

Hydrolysis Of

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Purification of extracellular amylolytic enzymes from the thermophilic fungus Thermomyces lanuginosus

Canadian Journal of Microbiology ◽

10.1139/m88-041 ◽

1988 ◽

Vol 34 (3) ◽

pp. 218-223 ◽

Cited By ~ 26

Author(s):

Bo Jensen ◽

Jorgen Olsen ◽

Knud Allermann

Keyword(s):

Molecular Weight ◽

Ion Exchange ◽

Soluble Starch ◽

Ion Exchange Chromatography ◽

Exchange Chromatography ◽

Thermomyces Lanuginosus ◽

Amylolytic Enzymes ◽

Molecular Weights ◽

Isoelectric Points ◽

Hydrolysis Of

When grown in static culture it appears as if Thermomyces lanuginosus has a biphasic secretion of the extracellular starch-degrading activity. This could be due to the presence of at least two different amylases. By ion-exchange chromatography on DEAE-Trisacryl an α-amylase (EC 3.2.1.1) and a glucoamylase (EC 3.2.1.3) were separated and purified from the extracellular protein from 14-day-old static cultures grown on soluble starch. The hydrolysis of soluble starch by the purified glucoamylase resulted in only glucose as the end product, whereas the α-amylase gave maltose as the smallest end product. The molecular weights and isoelectric points of the enzymes were for glucoamylase 70 000 – 76 000 and pH 4.0, and for α-amylase 54 000 – 57 000 and pH 3.4. An α-glucosidase (EC 3.2.1.20) with a molecular weight of 44 000 – 48 000 and an isoelectric point at pH 3.8 was eluted close to the α-amylase fraction on the DEAE-Trisacryl column.

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