The cloned ?-mannanase gene from alkalophilic Bacillus sp. AM-001 produces two ?-mannanases in Escherichia coli

Akino, Toshiro; Kato, Chiaki; Horikoshi, Koki

doi:10.1007/bf00447004

Cited by 16 publications

(15 citation statements)

References 18 publications

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“…Furthermore, a-galactosidase (EC 3.2.1.22) and fl-glucosidase (EC 3.2.1.21) are needed for the complete breakdown of hetero-mannans, fl-Mannanase and fl-mannosidases have been described from some microbial sources (Reese and Shibata 1965;Decker and Richards 1976;Pavlova and Tinyanova 1980;Ishihara and Shimizu 1980;Park et al 1987;Civas et al 1984), and fl-mannanase genes were recently cloned from an alkalophilic Bacillus sp. (Akino et al 1989) and the extremely thermophile Caldocellum saccharolyticum (Liithi et al 1991).…”

Section: Introductionmentioning

confidence: 99%

Purification, and characterization of a β-mannanase of Trichoderma reesei C-30

Arisan-Atac

Hodits

Kristufek

et al. 1993

Appl Microbiol Biotechnol

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Trichoderma reesei was studied for its ability to produce fl-mannanase activity on a variety of carbon sources. The highest fl-mannanase activity was produced on cellulose, whereas fl-mannan-containing carbon sources (such as konjac powder or locust bean gum) gave lower enzyme titres. The enzyme responsible for the major fl-mannanolytic activity from T. reesei was purified to physical homogeneity by preparative chromatofocusing and anion exchange fast protein liquid chromatography. This fl-mannanase is a glycoprotein, with a molecular mass of 46 (+ 2) kDa and an isoelectric point of 5.2. It has an optimal pH at 5.0 and broad pH stability (2.5-7.0). It is stable for 60 min at 55 ° C, and has an optimal temperature for activity at 75 ° C. During incubation with locust bean gum, the enzyme releases mainly tri-and disaccharides.

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Section: Introductionmentioning

confidence: 99%

Purification, and characterization of a β-mannanase of Trichoderma reesei C-30

Arisan-Atac

Hodits

Kristufek

et al. 1993

Appl Microbiol Biotechnol

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“…Jamb-602 ); Bc-K1, Bacillus circulans K1 (Yoshida et al 1998); and Bs-AM001, Bacillus sp. AM-001 (Akino et al 1989) hydrolase family 10 conserved domain from amino acids 37-305 (Henrissat and Bairoch 1996), and the residues that had previously been determined to be essential for catalysis were also present (E133 and E240) (Lee et al 1993;Moreau et al 1994;Tull et al 1991). This same region had high homology to 2 other bacterial xylanase enzymes (Fig.…”

Section: Resultsmentioning

confidence: 94%

“…1). Three of these mannanase enzymes are unique in that they are active at alkaline pH (Akino et al 1989;Ma et al 2004;Takeda et al 2004). Ma has postulated that this domain may impart the alkaline activity to these enzymes (Ma et al 2004).…”

Section: Resultsmentioning

confidence: 97%

Molecular cloning and characterization of multidomain xylanase from manure library

Kibblewhite

Orts

et al. 2009

World J Microbiol Biotechnol

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The gene (manf-x10) encoding xylanase from an environmental genomic DNA library was cloned and expressed in Escherichia coli. The manf-x10 encoded a predicted protein of 467 amino acids residues with a molecular mass of 50.3 kD. Sequence analysis of manf-x10 gene revealed that the N-terminus had high homology to the catalytic domain of other bacterial xylanase enzymes. The optimal pH and temperature for xylanase activity were 7.0 and 40°C, respectively. In the presence of 1 mM solution of Co 2? , Fe 2? , Mg 2? and Zn 2? , the relative xylanase activity was enhanced; however, it had almost no activity in the presence of 10 mM solution of Cu 2? . The apparent K m and V max values obtained for the hydrolysis of rye arabinoxylan were 2.8 mg/ml and 49.5 lmol/min/mg, respectively. The C-terminus of the enzyme had high homology to a domain of unknown function found in several mannanase enzymes. Biochemical characterization of the C-terminus of the enzyme revealed a previously unrecognized carbohydrate binding module.

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“…It provides obvious advantages for applications in the production of mannooligosaccharides from hemicelluloses as one of the growth factors of Bifidobacterium sp. (Ma et al 2004), in the manufacture of kraft pulp (Khanongnuch et al 1999;Sunna et al 2000) and in the detergent industry (Akino et al 1989;Ma et al 2004), where a high pH is usually required.…”

Section: Introductionmentioning

confidence: 98%

“…AM001 (Akino et al 1987(Akino et al , 1989. Another novel alkaline b-mannanase (ManA) was found in alkaliphilic Bacillus sp.N16-5 isolated from the sediment of Wudunur Soda Lake in Inner Mongolia and its encoding gene was then cloned (Ma et al 1991(Ma et al , 2004.…”

Section: Introductionmentioning

confidence: 99%

High level expression of a truncated β-mannanase from alkaliphilic Bacillus sp. N16-5 in Kluyveromyces cicerisporus

et al. 2010

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A truncated alkaline β-mannanase from alkaliphilic Bacillus sp. N16-5 (MAN330) was expressed and secreted in Kluyveromyces cicerisporus. The recombinant engineered strain for MAN330 production was stable during 80 generations, and the maximum yield of MAN330 reached 3,795 U/ml in 15 l fermenter. MAN330 exhibited similar pH optima, temperature optima, and substrate specificities to its full-length protein (MAN493). However, stability of MAN330 was about 7% higher than that of MAN493 from pH 9-11. MAN330 had about 10% higher stability than MAN493 from 60°C to 80°C.

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The cloned ?-mannanase gene from alkalophilic Bacillus sp. AM-001 produces two ?-mannanases in Escherichia coli

Cited by 16 publications

References 18 publications

Purification, and characterization of a β-mannanase of Trichoderma reesei C-30

Purification, and characterization of a β-mannanase of Trichoderma reesei C-30

Molecular cloning and characterization of multidomain xylanase from manure library

High level expression of a truncated β-mannanase from alkaliphilic Bacillus sp. N16-5 in Kluyveromyces cicerisporus

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