Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47-Reference-Cited by-同舟云学术

Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47

Published:1995-09 Issue:1 Volume:1252 Page:35-42
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Tonozuka Takashi,Mogi Shin-ichi,Shimura Yoichiro,Ibuka Akiko,Sakai Hiroshi,Matsuzawa Hiroshi,Sakano Yoshiyuki,Ohta Takahisa

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference32 articles.

1. Purification and some properties of a novel .ALPHA.-amylase produced by a strain of Thermoactinomyces vulgaris.

2. Enzymatic properties and action patterns of Thermoactinomyces vulgaris .ALPHA.-amylase.

3. A Neopullulanase-typeα-Amylase Gene fromThermoactinomyces vulgarisR-47

4. Catalytic properties of the cloned amylase from Bacillus licheniformis.

5. Purification and characterization of periplasmic alpha-amylase from Xanthomonas campestris K-11151

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