Purification and some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuber

Noman, Anwar; Hoque, Md. Asadul; Sen, Piku; Karim, Md. Rezaul

doi:10.1016/j.foodchem.2005.07.056

Cited by 30 publications

(45 citation statements)

References 18 publications

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“…These findings tend to suggest that high-molecular mass substrates containing the α-1,6 linkage were the better substrate for the enzyme except potato soluble starch. These results are similar to substrates specificity for Pachyrhizus erosus L. tuber α-amylase reported by Noman et al [20]. Nirmala and Muralikrishna [23] reported that the three α-amylases from malted finger millet had different affinity toward different sources of cereal starches.…”

Section: Resultssupporting

confidence: 89%

“…4), gave also a molecular weight of 42 kDa for the previously equilibrated with 20 mM acetate buffer pH 5.6 at a flow rate of 30 ml/h and 3 ml fractions enzyme. The molecular weight of α-amylase AI is in the same range of 38-45 kDa as previously reported for α-amylases from other sources [20][21][22].…”

Section: Resultssupporting

confidence: 74%

“…4). Generally, in plant by ionexchange and gel filtration chromatographies, a number of isoenzymes of α-amylases were separated such as three α-amylases from malted finger millet were purified using DEAE-Sephacyl and Sephacryl S-200 columns [19] and Noman et al [20] used two ion exchange columns (DEAE-and CM-cellulose) to purified Pachyrhizus erosus L. tuber α-amylase. By using Sephacryl S-200 column, the native molecular weight of orange peel α-amylase AI was found to be 42 kDa.…”

Section: Resultsmentioning

confidence: 99%

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Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Mohamed

Drees

El-Badry

et al. 2009

Appl Biochem Biotechnol

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alpha-Amylase activity was screened in the peel, as waste fruit, of 13 species and cultivars of Egyptian citrus. The species Citrus sinensis cv. Abosora had the highest activity. alpha-Amylase AI from Abosora peel was purified to homogeneity using anion and cation-exchange, and gel filtration chromatographies. Molecular weight of alpha-amylase AI was found to be 42 kDa. The hydrolysis properties of alpha-amylase AI toward different substrates indicated that corn starch is the best substrate. The alpha-amylase had the highest activity toward glycogen compared with amylopectin and dextrin. Potato starch had low affinity toward alpha-amylase AI but it did not hydrolyze beta-cyclodextrin and dextran. Apparent Km for alpha-amylase AI was 5 mg (0.5%) starch/ml. alpha-Amylase AI showed optimum activity at pH 5.6 and 40 degrees C. The enzyme was thermally stable up to 40 degrees C and inactivated at 70 degrees C. The effect of mono and divalent metal ions were tested for the alpha-amylase AI. Ba2+ was found to have activating effect, where as Li+ had negligible effect on activity. The other metals caused inhibition effect. Activity of the alpha-amylase AI was increased one and half in the presence of 4 mM Ca2+ and was found to be partially inactivated at 10 mM Ca2+. The reduction of starch viscosity indicated that the enzyme is endoamylase. The results suggested that, in addition to citrus peel is a rich source of pectins and flavanoids, alpha-amylase AI from orange peel could be involved in the development and ripening of citrus fruit and may be used for juice processing.

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Section: Resultssupporting

confidence: 89%

Section: Resultssupporting

confidence: 74%

Section: Resultsmentioning

confidence: 99%

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Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Mohamed

Drees

El-Badry

et al. 2009

Appl Biochem Biotechnol

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“…The optimal activity of DzAmy3 at pH 8.0 is in accordance with chloroplast α-amylase of AtAMY3 (pH 7.5-8.0). The plant α-amylases are highly active in acidic to neutral range (Ben Elarbi et al 2009;Kanwal et al 2004;Kumari et al 2010;Noman et al 2006;Tripathi et al 2007). We hypothesized that optimal activity at pH 8.0 is unique property for activity in the plastid stroma (Seung et al 2013).…”

Section: Organismmentioning

confidence: 94%

“…The high activity and stability of the enzyme under alkaline condition are good properties for detergent industries. The plant α-amylase generally exhibit optimal activity at 37-70°C (Ben Elarbi et al 2009;Kanwal et al 2004;Noman et al 2006) but at low temperature it shows low catalytic efficiency. The rDzAmy3 exhibits high catalytic efficiency even at low temperature, suggesting rDzAmy3 is cold-adapted α-amylase which is biocatalysts with broad ability in industrial applications (Kuddus et al 2012).…”

Section: Organismmentioning

confidence: 99%

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Posoongnoen

Ubonbal

Thammasirirak

et al. 2015

Plant Biotechnology

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Amylase is hypothesized to involve in the initiation of intracellular starch granule digestion in the plastids of ripening durians. A putative α-amylase from Mon Thong durian (Durio zibethinus Murr. cv. Mon Thong; DzAmy3) was successfully isolated and its gene contain a 2,679 base pair open reading frame, which encodes 892 amino acids with a calculated molecular mass of 93.7 kDa and an isoelectric point of 5.77. The DzAmy3 contains starch binding domain with a putative plastid transit peptide and α-amylase like domain. Phylogenetic tree analysis proved it into the family three of plant α-amylases. The predicted structural model proposed a catalytic triad (Asp611, Glu636 and Asp719) for general acid/base hydrolysis. Recombinant DzAmy3 (rDzAmy3) was successfully expressed in Escherichia coli. rDzAmy3 hydrolyzed starch and ethylidene-pNP-G7 which confirms the authenticity of DzAmy3 gene and functional α-amylase. The rDzAmy3 had an optimum activity at pH 8.0 and 30°C. It was stable in the pH range of 7-8 at 37°C, temperature range of 5-20°C and in the presence of 1% (v/v) Tween 20 and Triton X-100. Substrate specificity analysis revealed that rDzAmy3 was active toward β-limit dextrin, starch, amylopectin, amylose and glycogen.

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Characterization of corn, cassava, and commercial flours: Use of amylase‐rich flours of germinated corn and sweet potato in the reduction of the consistency of the gruels made from these flours—Influence on the nutritional and energy value

Tene

Klang

Houketchang

et al. 2019

Food Science & Nutrition

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Malnutrition appears in weaning age and is usually due to weaning food which is of low nutritional value. This problem led us to investigate the study of the physicochemical and functional properties of cassava flours and corn flours, and the fluidification of the gruels made from these flours by germinated yellow corn and sweet white potato flours. To do this, the approximate chemical composition, physical and functional properties, and ability of amylase‐rich flours to digest the starch in order to reduce consistency were evaluated. From these analyses, it emerges that the chemical composition, and physical and functional properties are influenced by the nature and the treatment undergone by the flours. It appears that the amylase‐rich flours that we used at a concentration of 1%–3% during the preparation of the gruels significantly reduced their consistencies. Given their strong liquefying power, this reduction was more marked with germinated corn flour where 1% permits to obtain desired consistency with 21.50 g of DM of bitter cassava flour, thereby multiplying the energy density and nutritional value of this flour by 5.18. It also appears that the action of flours rich in amylases was depending on the concentration, the nature of the flour, its composition, and the treatment undergone. In view of all these results, we can therefore consider the formulation of a weaning food with the consistency, and energy and nutritional value necessary for the proper growth of children.

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Purification and some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuber

Cited by 30 publications

References 18 publications

Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Characterization of corn, cassava, and commercial flours: Use of amylase‐rich flours of germinated corn and sweet potato in the reduction of the consistency of the gruels made from these flours—Influence on the nutritional and energy value

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Purification and some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuber

Cited by 30 publications

References 18 publications

Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

Biochemical Properties of α-Amylase from Peel of Citrus sinensis cv. Abosora

&#x3b1;-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Characterization of corn, cassava, and commercial flours: Use of amylase‐rich flours of germinated corn and sweet potato in the reduction of the consistency of the gruels made from these flours—Influence on the nutritional and energy value

Contact Info

Product

Resources

About

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression