Cloning, expression and characterization of endo‐β‐1,4‐mannanase from Aspergillus fumigatus in Aspergillus sojae and Pichia pastoris

Duruksu, Gökhan; Öztürk, Bengü; Biely, Peter; Bakır, Ufuk; Ögel, Zümrüt B.

doi:10.1002/btpr.104

Cited by 45 publications

(27 citation statements)

References 23 publications

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“…The specific activity of rMan5P1 was 1703.1 ± 101.2 U/mg, which is lower than that of MAN5A from Bispora sp. MEY-1 (3373 U/mg; Luo et al, 2009), and b-mannosidase from A. niger BK01 (2570 U/mg; Do et al, 2009), but significantly higher than that of Man5XZ7 from T. arenaria XZ7 (704.5 U/mg; Lu et al, 2013), MANN from A. sulphureus (366 U/mg;Chen et al, 2007), PpMan from A. fumigatus (350 U/mg; Duruksu et al, 2009), and Man5XZ3 from A. nidulans XZ3 (184.8 U/mg; Lu et al, 2014).…”

Section: Substrate Specificity and Kinetic Parametersmentioning

confidence: 96%

“…Until now, the thermophilic fungi Talaromyces leycettanus JCM12802 (Wang et al, 2014a), Aspergillus fumigatus IMI 385708 (Duruksu, Ozturk, Biely, Bakir, & Ogel, 2009), Aspergillus nidulans XZ3 (Lu et al, 2014), Humicola insolens Y1 (Luo et al, 2012), Thielavia arenaria XZ7 (Lu et al, 2013), and Rhizomucor miehei (Katrolia et al, 2013) have been reported be the ideal microbial sources of excellent b-mannanases.…”

Section: Introductionmentioning

confidence: 99%

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A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers

Yang

Shi

et al. 2015

Food Chemistry

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Section: Substrate Specificity and Kinetic Parametersmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers

Yang

Shi

et al. 2015

Food Chemistry

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“…In this study, recombinant Aspergillus sojae transformant 1 (AsT1) (DURUKSU et al, 2009) was used, which was obtained from Prof. Dr. Z.B. Ogel's laboratory (Middle East Technical University, Ankara, Turkey).…”

Section: Methodsmentioning

confidence: 99%

“…The stock culture was grown on potato dextrose agar (PDA) at 30 ºC for 4-5 days, stored at 4 ºC, and sub-cultured bi-monthly. Inoculum was prepared by washing each incubated PDA agar plate with 5 ml of sterile saline (0.8%, w/v) and Tween-80 (0.005%, v/v) mixed solution (DURUKSU et al, 2009;OZTURK et al, 2010). The resulting suspension solution had about 4.0×10 7 spores per ml.…”

Section: Methodsmentioning

confidence: 99%

Enhanced β-mannanase production from alternative sources by recombinant Aspergillus sojae

Yatmaz¹,

Karahalil²,

Germeç³

et al. 2016

Acta Alimentaria

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β-mannanases can degrade galactomannans to mannose and it has been used in various application areas. The aim of this study was to produce the β-mannanase from carob pod extract including different nitrogen sources. The best operation values for fermentation were determined to be 8% initial sugar concentration with 0.5% yeast extract, 100 r.p.m., and 7% inoculation rate, which yielded the maximum β-mannanase activity as 423.60 U ml -1 . Effects of nitrogen sources on β-mannanase activity were also studied and it reached 695.6 U ml -1 by using 0.5% of ammonium nitrate as the nitrogen source at the determined optimum conditions. Results also showed that meat bone meal and soybean meal could be used as cost effective nitrogen sources based on achieved β-mannanase activity.Keywords: β-mannanase, recombinant Aspergillus sojae, carbon sources, nitrogen sourcesMicrobial mannanase has gained signifi cant attention, since it degrades the complex polysaccharides of plant tissues into simple small molecules such as manno-oligosaccharides and mannose. For example, the increased availability and high specifi city of β-mannanases have been used for numerous applications, such as production of manno-oligosaccharides, pharmaceutical applications, instant coffee production, animal feeds, paper and pulp production, detergent formulations etc. ( VAN ZYL et al., 2010;LU et al., 2014). β-Mannanase could be generally produced by various Aspergillus species ( VAN ZYL et al., 2010) and the activity of the produced enzymes can differ from species to species. Also, other microorganisms have been evaluated for β-mannanase productions. CHEN and coworkers (2007) expressed Aspergillus sulphures β-mannanase gene in Pichia pastoris and the specifi c activity was found to be 366 U ml -1 in locust bean gum. OZTURK and co-workers (2010) used recombinant Aspergillus sojae ATCC11906 (AsT1) for β-mannanase production from molasses and found the highest activity value as 363 U ml -1. WANG and co-workers (2010) have found that Pantoea agglomerans A021 could produce β-mannanase from konjac powder and the maximum activity of purifi ed Man26P was 514 U mg -1. WU and co-workers (2011) used Aspergillus niger E-30 to produce the β-mannanase from peeled potato and the maximum β-mannanase activity value was 1067.5 U mg -1 by purifi ed enzyme solution

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“…For example, recombinant β-mannanases of Aspergillus sulphureus [14], Bispora sp. MEY-1 [15], and Aspergillus fumigatus [16] have been produced in Pichia pastoris and showed activity up to 500 U ml −1 . However, due to the limitations of knowledge for enzyme function, application of fungal mannanases is still confined.…”

Section: Introductionmentioning

confidence: 99%

A Novel endo-1,4-β-Mannanase from Bispora antennata with Good Adaptation and Stability over a Broad pH Range

Liu

Yang

Luo

et al. 2012

Appl Biochem Biotechnol

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An endo-β-1,4-mannanase encoding gene, man5, was cloned from Bispora antennata CBS 126.38, which was isolated from a beech stump. The cDNA of man5 consists of 1,299 base pairs and encodes a 432-amino-acid protein with a theoretical molecular mass of 46.6 kDa. Deduced MAN5 exhibited the highest amino acid sequence identity of 58% to a β-mannanase of glycoside hydrolase family 5 from Aspergillus aculeatus. Recombinant MAN5 was expressed in Pichia pastoris and purified to electrophoretic homogeneity. The specific activity of the final preparation towards locust bean gum was 289 U mg(-1). MAN5 showed optimal activity at pH 6.0 and 70 °C and had good adaptation and stability over a broad range of pH values. The enzyme showed more than 60% of peak activity at pH 3.0-8.0 and retained more than 80% of activity after incubation at 37 °C for 1 h in both acid and alkaline conditions (pH 4.0-11.0). The K (m) and V (max) values were 1.33 mg ml(-1) and 444 μmol min(-1) mg(-1) and 1.17 mg ml(-1) and 196 μmol min(-1) mg(-1) for locust bean gum and konjac flour, respectively. Of all tested metal ions and chemical reagents, Co(2+), Ni(2+), and β-mercaptoethanol enhanced the enzyme activity at 1 mM, whereas other chemicals had no effect on or partially inhibited the enzyme activity. MAN5 was highly resistant to acidic and neutral proteases (trypsin, α-chymotrypsin, collagenase, subtilisin A, and proteinase K). By virtue of the favorable properties of MAN5, it is possible to apply this enzyme in the paper and food industries.

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Cloning, expression and characterization of endo‐β‐1,4‐mannanase from Aspergillus fumigatus in Aspergillus sojae and Pichia pastoris

Cited by 45 publications

References 23 publications

A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers

A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers

Enhanced β-mannanase production from alternative sources by recombinant Aspergillus sojae

A Novel endo-1,4-β-Mannanase from Bispora antennata with Good Adaptation and Stability over a Broad pH Range

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