Synthesis of Maltosyl(α1→6)cyclodextrins through the Reverse Reaction of Thermostable Bacillus acidopullulyticus Pullulanase(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
Maltosyl(α1→6)α-, β- or γ-cyclodextrin was synthesized from maltose and α-, β- or γ-cyclodextrin, respectively, using Bacillus atidopullulyticus pullulanase (EC 3.2.1.41). More than 40% of each cyclodextrin substrate was converted to the corresponding maltosyl(α1→6)cyclodextrin under the conditions given below ; the combined concentration of maltose and cyclodextrin was 70〜75% (w/w), the molar ratio of maltose to cyclodextrin was 9〜18, and the amount of pullulanase was 100〜200units/g of cyclodextrin. The optimum pH and temperature for the formation of maltosyl(α1→6)cyclodextrins were 4.0〜4.5 and 60〜70℃, respectively. Each maltosyl(α1→6)-cyclodextrin produced was separated from noncyclic saccharides, maltose and branched tetraose, by methanol and ethanol precipitations. The maltosyl(α1→6)cyclodextrins were further purified by gel filtration on a Toyopearl HW 40S column and crystallization from aqueous (for maltosyl(α1→6)α-cyclodextrin) or methanol (for maltosyl(α1→6)β-cyclodextrin) solution. From 10 g each of the corresponding cyclodextrin, the yields of the purified maltosyl(α1→6)α-, β- and γ-cylcodextrins were 3.0〜3.6g, 2.5〜2.8g and 2.2〜2.5g, respectively. Identification of the maltosyl(α1→6)cyclodextrins was performed by means of hydrolysis with Klebsiella pneumonias pullulanase, methylation analysis and ^<13>C-NMR analysis.
- 社団法人日本農芸化学会の論文
- 1989-08-23
著者
-
Tsumuraya Yoichi
Department Of Biochemistry Faculty Of Science Saitama University
-
Tsumuraya Yoichi
Department Of Bilchemistry Faculty Of Science Saitama University
-
SAKANO Yoshiyuki
Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, To
-
Kusano Shuichi
(present Address)ohmiya Research Laboratory Nikken Chemicals Co. Ltd.
-
Kusano S
Research Institute Fuji Sangyo Co. Ltd.
-
Shiraishi T
Department Of Biotechnology Graduate School Of Engineering Osaka University
-
SHIRAISHI Takanori
Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Univ
-
KUSANO Shuichi
Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Univ
-
Sakano Y
Department Of Applied Biological Science Faculty Of Agriculture Tokyo University Of Agriculture And
-
Sakano Yoshiyuki
Laboratory Of Biochemistry Department Of Agricultural Chemistry Tokyo University Of Agriculture And
関連論文
- Mode of Action of β-Glucuronidase from Aspergillus niger on the Sugar Chains of Arabinogalactan-Protein
- Purification and Characterization of Intracellular Proteinases in Pleurotus ostreatus Fruiting Bodies
- Characterization of a Thermostable Lysine-Specific Metalloendopeptidase from the Fruiting Bodies of a Basidiomycete, Grifola frondosa
- Purification and Properties of a Lectin from the Fruitbodies(Biological Chemistry)
- Structures of Thermoactinomyces vulgaris R-47 α-Amylase II Complexed with Substrate Analogues
- The Deletion of Amino-Terminal Domain in Thermoactinomyces vulgaris R-47 α-Amylases : Effects of domain N on Activity, Specificity, Stability and Dimerization
- Analysis of Catalytic Residues of Thermoactinomyces vulgaris R-47 α-Amylase II (TVA II) by Site-directed Mutagenesis
- Purification, Characterization, and Subsite Affinities of Thermoactinomyces vulgaris R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases
- Construction of an Efficient Expression System for Aspergillus Isopullulanase in Pichia pastoris, and a Simple Purification Method(Biochemistry & Molecular Biology)
- Studies on the Hydrolyzing Mechanism for Cyclodextrins of Thermoactinomyces vulgaris R-47 α-Amylase 2 (TVAII). X-Ray Structure of the Mutant E354A Complexed with β-Cyclodextrin, and Kinetic Analyses on Cyclodextrins
- Enzymatic Deglycation of Fructosyl-lysine(Biological Chemistry)
- Chemical Modification of Sulfhydryl Groups in Porcine Pancreatic α-Amylase, and Purification and Properties of the Modified Amylase(Biological Chemistry)
- Quantitation of formate by solid-phase microextraction and gas chromatography-mass spectrometry utilizing a [^C]formate internal standard
- Methylamine Treatment Changes the Allocation of Carbohydrate to Roots in Rice Plants(ENVIRONMENTAL BIOTECHNOLOGY)
- Formate Dehydrogenase Gene of Arabidopsis thaliana is Induced by Formaldehyde and Not by Formic Acid
- Formate Protects Photosynthetic Machinery from Photoinhibition
- Subsite Structure and Mode of Action of Native and Modified α-Amylase from Poricine Pancreas(Biological Chemistry)
- Reddish Escherichia coli Cells Caused by Overproduction of Bacillus stearothermophilus Uroporphyrinogen III Methylase : Cloning, Sequencing, and Expression of the Gene
- A Neopullulanase-type α-Amylase Gene from Thermoactinomyces vulgaris R-47
- Enzymatic Preparation of Novel Non-reducing Oligosaccharides Having an Isomaltosyl Residue by Using the Transfer Action of Isomaltodextranase from Arthrobacter globiformis T6
- A 110-kDa WGA-binding Glycoprotein Involved in Cell Adhesion Acts as a Receptor for Aggregation Factor in Embryos of the Sea Urchin, Hemicentrotus pulcherrimus(Developmental Biology)
- Isolation of Antidiabetic Components from White-Skinned Sweet Potato (Ipomoea batatas L.)
- Purification and Properties of Glucosyltransferase Produced by Streptococcus salivarius HHT
- Immobilization of Bacillus acidopullulyticus Pullulanase and Properties of the Immobilized Pullulanases
- Synthesis of Maltosyl(α1→6)cyclodextrins through the Reverse Reaction of Thermostable Bacillus acidopullulyticus Pullulanase(Biological Chemistry)
- Purification and Properties of Bacillus acidopullulyticus Pullulanase (Biological Chemistry)
- AMOR, a 70-kDa protein from the ovule, induces competence of the pollen tube to respond to the final-step guidance
- Specific Localizaiton of Arabinogalactan-Protein Epitopes at the Surface of Maize Root Hairs
- In Vitro Biosynthesis of Homogalacturonan by a Membrane-bound Galacturonosyltransferase from Epicotyls of Azuki Bean(Biochemistry & Molecular Biology)
- Synthesis of Branched α-Cyclodextrin Carrying a Side Chain Longer than Maltose Using Bacillus acidopullulyticus Pullulanase(Biological Chemistry)
- Uptake of ^3H-Cortisol by Isolated Liver Nuclei Obtained from Hypophysectomized Rat
- Preparation and Enzymatic Hydrolysis of Maltosyl-α-cyclodextrin
- -0351-THE EFFECT OF INIERLEUKIN-6 ON PROLIFERATION OF CULTURED VASCULAR SMOOTH MUSCLE CELLS
- An Arabinogalactan-protein from Rape Leaves
- Immunological Properties of Arabinogalactan Proteins from Leaves of Cruciferous Plants
- Purification and Properties of an exo-α-Amylase from Pseudomonas stutzeri
- Purification of a-Maltotetraose-forming exo-Amylase of Pseudomonas stutzeri-Two-forms of the Amylase and Their Enzymatic Properties
- Hydrolysis of α-1, 4- and α-1, 6-Glucosidic Linkages in Trisaccharides by the Thermoactinomyces vulgaris α-Amylase
- Hydrolysis of α-1, 6-Glucosidic Linkages by α-Amylases
- Characterization of a Thermostable Lysine-Specific Metalloendopeptidase from the Fruiting Bodies of a Basidiomycete, Grifola frondosa.