Biochemical characteristics of C-terminal region of recombinant chitinase from Bacillus licheniformis- implication of necessity for enzyme properties

Research background. Cellulose is an ingredient of waste materials that can be converted to other valuable substances. This is possible provided that, the polymer molecule will be degraded to smaller particles, used as a carbon source by microorganisms. Because of the frequently applied methods of pre-treatment of lignocellulosic materials, the cellulases derived from thermophilic microorganisms are particularly desirable. Experimental approach. We were looking for cellulolytic microorganisms able to grow at 50 °C. We described their morphological features and biochemical characteristics based on CMCase activity and the api®ZYM. The growth curves, during incubation at 50 °C, were examined using the microbioreactor BioLector®. Results and conclusions. 40 bacterial strains were isolated from fermenting hay, geothermal karst spring, hot spring and geothermal pond at 50 °C. The vast majority of the bacteria were Gram-positive and rod-shaped with the maximum growth temperature of at least 50 °C. We also demonstrated a large diversity of biochemical characteristics among the microorganism. The CMCase activity was confirmed for 27 strains. However, the hydrolysis capacities (HC) were significant in bacterial strains: BBLN1, BSO6, BSO10, BSO13 and BSO14, and reached 2.74, 1.62, 1.30, 1.38 and 8.02 respectively. Rapid and stable growth was presented, among others, by BBLN1, BSO10, BSO13 and BSO14. The strains fulfilled the selection conditions and were identified based on the 16S rDNA sequences. BBLN1, BSO10, BSO13 were classified as Bacillus licheniformis, whereas BSO14 as Paenibacillus lactis. Novelty and scientific contribution. We described cellulolytic activity and biochemical characteristics of many bacteria isolated from hot environments. We are also the first to report the cellulolytic activity of thermotolerant P.s lactis. Described strains can be a source of new thermostable cellulases, which are extremely desirable in various branches of the circular bioeconomy.

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Improved enzyme properties upon glutaraldehyde cross-linking of alginate entrapped xylanase from Bacillus licheniformis

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2017.01.104 ◽

2017 ◽

Vol 98 ◽

pp. 24-33 ◽

Cited By ~ 31

Author(s):

Sharad Kumar ◽

Izharul Haq ◽

Jyoti Prakash ◽

Abhay Raj

Keyword(s):

Bacillus Licheniformis ◽

Cross Linking ◽

Enzyme Properties

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Molecular and Biochemical Characteristics of Recombinant β-Propeller Phytase from Bacillus licheniformis Strain PB-13 with Potential Application in Aquafeed

Applied Biochemistry and Biotechnology ◽

10.1007/s12010-014-0871-9 ◽

2014 ◽

Vol 173 (2) ◽

pp. 646-659 ◽

Cited By ~ 11

Author(s):

Vinod Kumar ◽

Punesh Sangwan ◽

A. K. Verma ◽

Sanjeev Agrawal

Keyword(s):

Bacillus Licheniformis ◽

Potential Application ◽

Biochemical Characteristics

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Expression and Biochemical Characteristics of a Phospholipase D from Bacillus licheniformis

Journal of Applied Biological Chemistry ◽

10.3839/jabc.2011.017 ◽

2011 ◽

Vol 54 (2) ◽

pp. 94-100 ◽

Cited By ~ 2

Author(s):

Han-Chul Kang ◽

Sang-Hong Yoon ◽

Chang-Muk Lee ◽

Bon-Sung Koo

Keyword(s):

Bacillus Licheniformis ◽

Phospholipase D ◽

Biochemical Characteristics

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Microanatomy of the Periplasm of Bacillus Licheniformis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065365 ◽

1971 ◽

Vol 29 ◽

pp. 262-263

Author(s):

B.K. Ghosh

Keyword(s):

Cell Wall ◽

Plasma Membrane ◽

Bacillus Licheniformis ◽

External Environment ◽

Permeability Barrier ◽

Periplasmic Space ◽

Modified Technique ◽

Gram Positive ◽

Gram Negative ◽

Gram Positive Bacteria

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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