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      Production and characterization of cyclodextrin glycosyltransferase from Bacillus sp. isolated from Cuban soil

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          Abstract

          A cyclodextrin glycosyltransferase (CGTase) from an alkaliphilic Bacillus sp. strain, isolated from Cuban soil, was purified with Sephadex G-50 with a yield of 66.5%. The CGTase was stable over a very wide pH range, 6.0–10, at 25°C and was most active at pH 7.5. The enzyme exhibited an optimum temperature of 60°C and was stable to 50°C for at least 8 h. The T 50 value – defined as the temperature at which 50% of the initial activity was retained–was 63°C in this enzyme. The influence of substrate or product concentration on the initial rate of CD production was studied, and the kinetic parameters were determined. The analysis of kinetic parameters K m and V max was obtained by the action of CGTase on the starch of corn with respect to β-CD, and the values were 4.1 g/L and 5.2 μM β-CD/min ml, respectively. The purified CGTase from Bacillus sp. could be used for an efficient cyclodextrin (CD) production which is the significant yield of γ- CDs.

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          Most cited references 41

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          Developments in the use of Bacillus species for industrial production.

          Bacillus species continue to be dominant bacterial workhorses in microbial fermentations. Bacillus subtilis (natto) is the key microbial participant in the ongoing production of the soya-based traditional natto fermentation, and some Bacillus species are on the Food and Drug Administration's GRAS (generally regarded as safe) list. The capacity of selected Bacillus strains to produce and secrete large quantities (20-25 g/L) of extracellular enzymes has placed them among the most important industrial enzyme producers. The ability of different species to ferment in the acid, neutral, and alkaline pH ranges, combined with the presence of thermophiles in the genus, has lead to the development of a variety of new commercial enzyme products with the desired temperature, pH activity, and stability properties to address a variety of specific applications. Classical mutation and (or) selection techniques, together with advanced cloning and protein engineering strategies, have been exploited to develop these products. Efforts to produce and secrete high yields of foreign recombinant proteins in Bacillus hosts initially appeared to be hampered by the degradation of the products by the host proteases. Recent studies have revealed that the slow folding of heterologous proteins at the membrane-cell wall interface of Gram-positive bacteria renders them vulnerable to attack by wall-associated proteases. In addition, the presence of thiol-disulphide oxidoreductases in B. subtilis may be beneficial in the secretion of disulphide-bond-containing proteins. Such developments from our understanding of the complex protein translocation machinery of Gram-positive bacteria should allow the resolution of current secretion challenges and make Bacillus species preeminent hosts for heterologous protein production. Bacillus strains have also been developed and engineered as industrial producers of nucleotides, the vitamin riboflavin, the flavor agent ribose, and the supplement poly-gamma-glutamic acid. With the recent characterization of the genome of B. subtilis 168 and of some related strains, Bacillus species are poised to become the preferred hosts for the production of many new and improved products as we move through the genomic and proteomic era.
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            A rapid and sensitive method of microgram quantities of protein utilizing the principle of protein-dye binding

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              Supramolecular chemistry of cyclodextrins in enzyme technology.

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                Author and article information

                Contributors
                (View ORCID Profile)
                Journal
                SOR-CHEM
                ScienceOpen Research
                ScienceOpen
                2199-1006
                02 December 2014
                : 0 (ID: e17a3de1-54f3-492e-80ee-21ac1d835fda )
                : 0
                : 1-6
                Affiliations
                [1 ]Center for Enzyme Technology, University of Matanzas, Matanzas, Cuba
                Author notes
                [* ]Corresponding author's e-mail address: hlrperez2003@ 123456gmail.com
                Article
                2176:XE
                10.14293/S2199-1006.1.SOR-CHEM.ASGLIM.v1
                © 2014 K.H. Sánchez et al.

                This work has been published open access under Creative Commons Attribution License CC BY 4.0 , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Conditions, terms of use and publishing policy can be found at www.scienceopen.com .

                Page count
                Figures: 6, Tables: 1, References: 40, Pages: 6
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