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Ammar, Youssef Ben,Matsubara, Takayoshi,Ito, Kazuo,Iizuka, Masaru,Limpaseni, Tipaporn,Pongsawasdi, Piamsook,Minamiura, Noshi 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.6
An $\alpha$-amylase (EC 3.2.1.1) was purified that catalyses the production of a high level of maltose from starch without the attendant production of glucose. The enzyme was produced extracellularly by thermophilic Streptomyces sp. that was isolated from Thailand's soil. Purification was achieved by alcohol precipiation, DEAE-Cellulose, and Gel filtration chromatographies. The purified enzyme exhibited maximum activity at pH 6-7 and $60^{\circ}C$. It had a relative molecular mass of 45 kDa, as determined by SDS-PAGE. The hydrolysis products from starch had $\alpha$-anomeric forms, as determined by $^1H$-NMR. This maltose-forming $\alpha$-amylase completely hydrolyzed the soluble starch to produce a high level of maltose, representing up to 90%. It hydrolyzed maltotetrose and maltotriose to primarily produce maltose (82% and 62%, repectively) without the attendant production of glucose. The high maltose level as a final end-product from starch and maltooligosaccharides, and the unique action pattern of this enzyme, indicate an unusual maltose-forming system. After the addition of the enzyme in the bread-baking process, the bread's volume increased and kept its softness longer than when the bread had no enzyme.
( Youssef Ben Ammar ),( Takayoshi Matsubara ),( Kazuo Ito ),( Masaru Lizuka ) 생화학분자생물학회 2002 BMB Reports Vol.35 No.6
An α-amylase(EC 3.2.1.1) was purified that catalyses the production of a high level of maltose from starch without the attendant production of glucose. The enzyme was produced extracellularly by thermophilic Streptomyces sp. that was isolated from Thailand`s soil. Purification was achieved by alcohol precipitation, DEAE-Cellulose, and Gel filtration chromatographies. The purified enzyme exhibited maximum activity at PH 6-7 and 60℃. It had a relative molecular mass of 45 kDa, as determined by SDS-PAGE. The hydrolysis products from starch had α-anomeric forms, as determined by ^1H-NMR. This-maltose-forming α-amylase completely hydrolyzed the soluble starch to produce a high level of maltose, representing up to 90%. It hydrolyzed maltotetrose and maltotriose to primarily produce maltose (82% and 62%, respectively) without the attendant production of glucose. The high maltose level as a final end-product from starch and maltooligosaccharides, and the unique action pattern of this enzyme, indicate an unusual maltose-forming system. After the addition of the enzyme in the bread-baking process, the bread`s volume increased and kept its softness longer than when the bread had no enzyme.
Mabrouk Ben Brahim,Hafedh Belhadj Ammar,Ridha Abdelhédi,Youssef Samet 한국화학공학회 2016 Korean Journal of Chemical Engineering Vol.33 No.9
The removal of pesticides from water is a major environmental concern. This study investigates the electrochemical removal of the insecticide imidacloprid (IMD) from aqueous solutions on a boron-doped diamond (BDD) and Ta/PbO2 anodes under galvanostatic electrolysis. The influence of operating parameters, such as applied current density (50-100 mA cm−2), initial chemical oxygen demand COD (0) (281-953mg L−1), temperature (25-65 oC) and pH (3.0-10.0) on COD and instantaneous current efficiency (ICE), was studied using the BDD electrode. The degradation efficiency of IMD increased by increasing current density and temperature, but noticeably decreased by the increase of initial pH value and initial concentration of IMD. The COD decay follows a pseudo-first-order kinetic, and the process was under mass transport control. COD removal reaches 90% when using an apparent current density of 100mA cm−2, initial COD of 953mg L−1, pH of 3.0 and at 25 oC after 4.5 h electrolysis time. Compared with Ta/PbO2, BDD anode has shown better performance and rapidity in the COD removal using the same electrolysis device.
Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11
( Takayoshi Matsubara ),( Youssef Ben Ammar ),( Trisanti Anindyawati ),( Satoru Yamamoto ),( Kazuo Ito ),( Masaru Iizuka ),( Noshi Minamiura ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.4
Raw-starch-digesting α-amylase (Amyl Ⅲ) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT 11 using wheat bran in the medium. The purified Amyl Ⅲ digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl Ⅲ were maltotriose and maltose, although a small amount of glucose was produced. Amyl Ⅲ acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl Ⅲ on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl Ⅲ and GA I was observed for the digestion of raw starch granules.
Matsubara, Takayoshi,Ammar, Youssef Ben,Anindyawati, Trisanti,Yamamoto, Satoru,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.4
Complementary DNAs encoding $\alpha$-amylases (Amyl I, Amyl III) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl III that was a raw starch digesting $\alpha$-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 63.3% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the raw-starch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.
( Takayoshi Matsubara ),( Youssef Ben Ammar ),( Trisanti Anindyawati ),( Satoru Yamamoto ),( Kazuo Ito ),( Masaru Iizuka ),( Noshi Minamiura ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.4
Complementary DNAs encoding α-amylases (Amyl I, Amyl Ⅲ) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl Ⅲ that was a raw starch digesting α-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 633% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the rawstarch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.
Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11
Matsubara, Takayoshi,Ammar, Youssef Ben,Anindyawati, Trisanti,Yamamoto, Satoru,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.4
Raw-starch-digesting $\alpha$-amylase (Amyl III) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT-11 using wheat bran in the medium. The purified Amyl III digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl III were maltotriose and maltose, although a small amount of glucose was produced. Amyl III acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl III on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl III and GA I was observed for the digestion of raw starch granules.