Purification and Some Properties of Maltases I and II from Thermophilic Bacillus sp. KP 1035

スポンサーリンク

概要

• 論文の詳細を見る

• Two extracellular maltases, designated maltases I and II, were purified 25-and 210-fold from thermophilic Bacillus sp. KP 1035,respectively. The estimated molecular weights of maltases I and II were 53,000 and 43,000,respectively. On electrophoresis, maltase I migrated toward the anode faster than maltase II. The pH and temperature optima of both enzymes was 6.8 and 65℃. The apparent activation energy(kcal/mole)was : for maltase I, 41(30 to 43℃)and 19(43 to 65℃); for matase II, 26(30 to 45℃)and 16(45 to 65℃). The maltases were highly specific for α-1,4-glucosidic linkages. The hydrolysis rate of substrates diminished in the order : maltose, maltotriose, and phenyl-α-D-maltoside. α-1,4-Linkages of starch, amylose, β-cyclodextrin, and panose were not cleaved. The respective K_m values for maltose and maltotriose were 4.2 and 1.8 mM with maltase I, and 4.4 and 6.0 mM with maltase II. Tris(hydroxymethyl)aminomethane inhibited competitively maltases I and II; the K_i values were 0.43 and 0.35 mM, respectively. Glucono-δ-lactone inhibited both enzymes : two molecules of glucono-δ-lactone competed with one molecule of maltose for an activesite. p-Nitrophenyl-α-D-xylopyranoside was a noncompetitive inhibitor. The enzymes were inhibited by p-chloromercuribenzoate. Both maltases were stable up to 60℃. The pH range for stability of maltase I was 4.6 to 10.3 at 25℃ and 5.5 to 8.0 at 55℃; that of maltase II 5.4 to 9.8 at 25℃ and 6.2 to 7.6 at 55℃. Neither enzyme was inactivated after 18 hr at 25℃ in 6.2 M urea, but both were completely destroyed after 18 hr at 55℃ in 1.8 M urea.

• 公益社団法人日本生物工学会の論文
• 1978-04-25

著者

• Suzuki Yuzuru

  Department Of Applied Biochemistry Kyoto Prefectural University

• Abe Shigeo

  Department Of Agricultural Chemistry Kyoto Prefectural University

• IKEMOTO TOSHIO

  Department of Agricultural Chemistry, Kyoto Prefectural University

• Ikemoto Toshio

  Department Of Agricultural Chemistry Kyoto Prefectural University

• Suzuki Yuzuru

  Department Of Agricultural Chemistry Kyoto Prefectural University

関連論文

• Molecular approach to species identification of eggs with respect to determination of the spawning site of the Japanese eel Anguilla japonica
• Differential expression of two gonadotropin (GTH) β subunit genes during ovarian maturation induced by repeated injection of salmon GTH in the Japanese eel Anguilla japonica
• IMMUNOHISTOCHEMICAL IDENTIFICATION OF HYPERGLYCEMIC HORMONE -PRODUCING CELLS AND MOLT- INHIBITING HORMONE -PRODUCING CELLS IN THE EYESTALK OF THE KURUMA PRAWN, PENAEUS JAPONICUS
• Time-course response of plasma testosterone and estradiol-17β to salmon gonadotropin treatment in the Japanese eel during ovarian development
• Adequate interval of sGTH administration to induce vitellogenesis, and induction of ovulation by simultaneous administration of sGTH and 17α-hydroxyprogesterone in the Japanese eel
• Hemolymph vitellogenin levels during ovarian development in the kuruma prawn Penaeus japonicus
• Purification and characterization of vitellin from the ovary of kuruma prawn, Penaeus japonicus
• Use of an Emulsion Prepared with Lipophilized Gelatin for the Induction of Ovarian Maturation in the Japanese Eel Anguilla japonica
• USE OF AN EMULSION PREPARED WITH LIPOPHILIZED GELATIN FOR INDUCTION OF GONADAL MATURATION IN THE JAPANESE EEL, Anguilla japonica
• Vitellogenin Production Induced by Eyestalk Ablation in Juvenile Giant Freshwater Prawn Macrobrachium rosenbergii and Trial Methyl Farnesoate Administration
• Oral immunization specifically inhibits intestinal protein uptake in the common carp Cyprinus carpio L.
• Effects of Steroids on the Antibody Producing Activity of Lymphocytes in Rainbow Trout
• Changes in Immunoglobulin Producing Cells in Response to Gonadal Maturation in Rainbow Trout
• Humoral Immune Response Against Orally Administered Human γ Globulin in the Carp
• ACTIONS OF A GONADOTROPIN-RELEASING HORMONE ANTAGONIST ON GONADOTROPIC HORMONE RELEASE IN RAINBOW TROUT, Oncorhynchus mykiss
• DOPAMINERGIC REGULATION OF THE RELEASE OF GONADOTROPIN FROM DISPERSED PITUITARY CELLS OF TESTOSTERONE-TREATED IMMATURE RAINBOW TROUT, Oncorhynchus mykiss
• Molecular Determinants of Substrate Recognition in Thermostable α-glucosidases Belonging to Glycoside Hydrolase Family 13
• Immunoglobulin Concentration and Specific Antibody Activity in Oocytes and Eggs of Immunized Red Sea Bream
• Immunoglobulin in Oocytes, Fertilized Eggs, and Yolk Sac Larvae of Red Sea Bream
• Immunohistochemical identification of hyperglycemic hormone- and molt-inhibiting hormone-producing cells in the eyestalk of the kuruma prawn, Penaeus japonicus
• Transfer of Maternal Antibody from Mother to Egg may have no Protective Meaning for Larvae of Red Sea Bream Pagrus major, a Marine Teleost
• Identification of Catalytic and Substrate-binding Site Residues in Bacillus cereus ATCC7064 Oligo-1, 6-glucosidase(Biochemistry & Molecular Biology)
• The proline rule : A strategy for protein thermal stabilization
• Purification and Some Properties of Maltases I and II from Thermophilic Bacillus sp. KP 1035
• A general principle of increasing protein thermostability.

もっと見る 閉じる

スポンサーリンク