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南浦能至,安龍根,金俊平,吳文憲 中央大學校 食糧資源硏究所 1991 食糧資源硏究所 論文集 Vol.3 No.1
정제된 밀 β-amylase F-A 및 F-C의 단백질 화학적 및 효소 화학적 특성을 검토하였다. 정제 효소는 F-A, F-C 모두 SDS 전기영동 결과 분자량 54,500, 등전점은 F-A가 4.96, F-C가 4.61이고 아미노酸 殘基數는 F-A가 효소 1mole당 약 522잔기, F-C가 약 526잔기이다. ??, ?? 이온은 효소 F-A, F-C의 活性을 增加시켰으나 ??, ??, ??, ??이온은 효소 활성을 저해하였다. 작용 최적 pH는 F-A, F-C 모두 6.0이였다. 안정 pH영역은 pH4.5에서 7.5까지이고 작용 최적온도는 F-A, F-C 모두 50℃이며 안정온도 범위는 60℃이하로 나타났다. Km값은 가용성 전분에 대해 F-A가 0.19%, F-C가 0.56%로 나타났다. Beta-amylase(β-1, 4-D-glucan maltohydrolase, E. C. 3. 2. 1. 2.) from wheat (triticum aestivum var. Gerumil) produced in Korea was purified. The homogenity of purified wheat beta-amylase was indentified by P A G E. Enzymatic physico-chemical properties of the beta-amylase were investigated. The results thus obtains were as follows. The molecular weight of wheat beta-amylase determined by the S D S electrophoresis was 54,500 daltons. Isoelectric point of wheat beta-amylase for Fraction A and C were 4.96 and 4.61, respectively. Amino acid residues of wheat beta-amylase Fraction A and C were estimated to be around 522 and 526 per mol of enzyme, respectively. Wheat beta-amylase activity was increased by Ca?? and Mg?? ions, while it was inhibited by Hg??, Cu??, Ag??? and Fe??? ions. Km values of wheat beta-amylase Fraction A and C for soluble starch were 0.19 and 0.56%, respectively. The optimum pH and temperature of wheat beta-amylase Fraction A and C were 6.0 and 55℃. The enzyme were stable at pH 4.5 through 7.5 at below 50℃.
IO_4-산화 전분 변형 β-아밀라아제의 안정성 및 α-Cyclodextrin의 영향
安龍根,南浦能至 한국식품영양학회 1998 韓國食品營養學會誌 Vol.11 No.2
고구마 β-아밀라아제를 NaIO_4-산화 가용성 전분으로 변형하여 안정성을 측정하였다. 그 결과, 최적안정 pH는 3 및 4를 나타냈고, pH 3, 5∼9, 11에서 비변형 효소보다 높은 안정성을 나타냈다. 60℃에서 15분동안 변형효소는 비변형 효소보다 안정성이 증가하였다. 변형 보리 β-아밀라아제는 전체 pH에 걸쳐서 넓은 pH 안정성을 나타냈고, α-cyclodextrin은 이를 더욱 증가시켰다. pH stability of sweet potato β-amylase modified with IO_4-oxidized soluble starch was increased at pH 3, 5∼9 and 11. And optimum pH was 3 and 5 for modification. Thermal stability of the enzyme modified with IO_4-oxidized soluble starch was increased at 60℃ for 15min. pH stability of barley β-amylase modified with IO_4-oxidized soluble starch was increased at 3∼4 and 8∼11, and more increased at pH 3 and 8∼11 in the presence of α-cyclodextrin.
Stabilization of Amylolytic Enzymes by Modification with Periodate-Oxidized Soluble Starch
Ann, Yong-Geun,Anindyawati, Trisaniti,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi 한국식품영양학회 1998 韓國食品營養學會誌 Vol.11 No.5
The stabilization of amylolytic enzyme such as β-amylase of barley, β-amylase of wheat, β-amylase of sweet potato, α-amylase of Bacillus licheniformis, α-amylase of Aspergillus sp. and α-glucosidase of Aspergillus awamori was attained by modification with periodate-oxidized soluble starch. The pH stability of modified enzyme was increased at pH 9 for β-amylase of sweet potato, pH 3∼5 and 8∼11 for β-amylase of barley, pH 2∼3 and 7∼12 for β-amylase of wheat and pH 6 for α-glucosidase of Aspergillus awamori. Thermal stability increased 17.6% for α-amylase of Aspergillus sp. at 60℃ for 10min, 30% for α-amylase of Bacillus licheniformis at 100℃ for 5min and 4.5% for α-amylase of sweet potato at 60℃ for 10min compared with those of native enzymes.
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.
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.
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.
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.
( 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.