دورية أكاديمية

High-level production of a cold-active B-mannanase from Bacillus subtilis BS5 and its molecular cloning and expression.

التفاصيل البيبلوغرافية
العنوان: High-level production of a cold-active B-mannanase from Bacillus subtilis BS5 and its molecular cloning and expression.
المؤلفون: Huang JL; College of Bioengineering, Chonqing University, Chongqing 400044. huang_junli@126.com, Bao LX, Zou HY, Che SG, Wang GX
المصدر: Molekuliarnaia genetika, mikrobiologiia i virusologiia [Mol Gen Mikrobiol Virusol] 2012 (4), pp. 14-7.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Meditsina Country of Publication: Russia (Federation) NLM ID: 9315607 Publication Model: Print Cited Medium: Print ISSN: 0208-0613 (Print) Linking ISSN: 02080613 NLM ISO Abbreviation: Mol Gen Mikrobiol Virusol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Moskva : Meditsina,
مواضيع طبية MeSH: Enzyme Stability* , beta-Mannosidase*/chemistry , beta-Mannosidase*/genetics , beta-Mannosidase*/metabolism, Bacillus subtilis/*enzymology, Cloning, Molecular ; Cold Temperature ; Escherichia coli ; Gene Expression Regulation, Bacterial ; Sequence Analysis, DNA ; Temperature
مستخلص: Mannanases can be useful in the food, feed, pulp and paper industries. In this research a Bacillus subtilis strain (named Bs5) which produced high-level beta-mannanase was isolated. Maximum level of beta-mannanase (1231.41 U/ml) was reached when Bacillus subtilis Bs5 was grown on konjac powder as the carbon source for nine hours at 32 degrees C. The beta-mannanase was a typical cold-active enzyme and its optimal temperature of 35 degrees C was the lowest among those of the known mannanases from bacteria. In addition, the optimal pH was 5.0 and much wide pH range from 3.0-8.0 was also observed in the beta-mannanase. These properties make the beta-mannanase more attractive for biotechnological applications. The DNA sequence coding the beta-mannanase was cloned and the open reading frame consisted of 1089 bp encoding 362 amino acids. A phylogenetic tree of the beta-mannanase based on the similarity of amino acid sequences revealed that the beta-mannanase formed a cluster with the beta-mannanases of Bacillus subtilis, which was separated from the mannanases of fungi and other bacteria. The beta-mannanase gene could be expressed in Escherichia coli and the recombinant beta-mannanase was characterized by Western blot. This study provided a new source of carbohydrate hydrolysis enzyme with novel characteristics from Bacillus subtilis.
المشرفين على المادة: EC 3.2.1.25 (beta-Mannosidase)
تواريخ الأحداث: Date Created: 20121220 Date Completed: 20130213 Latest Revision: 20121219
رمز التحديث: 20231215
PMID: 23248847
قاعدة البيانات: MEDLINE