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

Yang, Hong; Shi, Pengjun; Lu, Haiquan; Wang, Huimin; Luo, Huiying; Huang, Huoqing; Yang, Peilong; Yao, Bin

doi:10.1016/j.foodchem.2014.10.022

Cited by 58 publications

(38 citation statements)

References 32 publications

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“…This result is comparable with Hakamada et al (2014) and Blibech et al (2011). Recently, β-mannanase from thermophilic fungus Neosartorya fischeri P1 (Yang et al 2015) significantly hydrolysed both konjac gum and LBG and generated mannose, M 2 , M 3 , M 4 , M 5 and M 6 with very low amount of M 4 while in this study β-mannanase produced M 3 and M 4 from LBG. Lack of mannose formation from LBG suggested that M. cinnamomea produced highly endo active β-mannanase without any associated β-mannosidase activity, a property important in generation of MOS.…”

Section: Resultsmentioning

confidence: 46%

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Experimental design of response surface methodology used for utilisation of palm kernel cake as solid substrate for optimised production of fungal mannanase

et al. 2016

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The results obtained from this work strongly indicate that the solid state fermentation (SSF) system using the palm kernel cake (PKC) as a substrate is an economical method for the production of β-mannanase at extremely low operational cost based on the fact that PKC is one of the cheap and abundant agro-waste by-products of the palm oil industry. Under initial conditions, i.e. 2 mm particle size of PKC, the moisture ratio of 1:1 of PKC:moistening agent and pH 7, Malbranchea cinnamomea NFCCI 3724 produced 109 U/gram distribution of the substrate (gds). The production of β-mannanase was optimised by the statistical approach response surface methodology (RSM) using independent variables, namely initial moisture (12.5), pH (9.0) and solka floc (100 mg). Noticeably, six fold enhancement of β-mannanase production (599 U/gds) was obtained under statistically optimised conditions. HPLC results revealed that β-mannanase is an endo-active enzyme that generated manno-oligosaccharides with a degree of polymerisation (DP) of 3 and 4. Semi-native PAGE analysis revealed that M. cinnamomea produced three isoforms of mannanase. Selective production of oligosaccharide makes M. cinnamomea β-mannanase an attractive enzyme for use in food and nutraceutical industries.

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Section: Resultsmentioning

confidence: 46%

“…However, only a few thermostable β-mannanases have been characterised from these (Puchart et al 2004; Yang et al 2015). Keeping this point in mind we evaluated a thermophilic fungus, M. cinnamomea NFCCI 3724 for optimised production of β-mannanase on PKC using the response surface methodology approach.…”

Section: Introductionmentioning

confidence: 99%

Experimental design of response surface methodology used for utilisation of palm kernel cake as solid substrate for optimised production of fungal mannanase

et al. 2016

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“…3). The main hydrolysis products of locust bean gum and konjac flour have been reported as galactose-branched mannooligosaccharides (17) and glucose-linked mannooligosaccharides (18). In the case of Man113A, a larger amount of shorter sugars was detected in the hydrolysis products of locust bean gum while higher hydrolytic activities (defined by the total reduced sugar equivalents) were detected when using konjac flour as the substrate.…”

Section: Resultsmentioning

confidence: 99%

A Novel Glycoside Hydrolase Family 113 Endo-β-1,4-Mannanase from Alicyclobacillus sp. Strain A4 and Insight into the Substrate Recognition and Catalytic Mechanism of This Family

Xia

et al. 2016

Appl Environ Microbiol

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c Few members of glycoside hydrolase (GH) family 113 have been characterized, and information on substrate recognition by and the catalytic mechanism of this family is extremely limited. In the present study, a novel endo-␤-1,4-mannanase of GH 113, Man113A, was identified in thermoacidophilic Alicyclobacillus sp. strain A4 and found to exhibit both hydrolytic and transglycosylation activities. The enzyme had a broad substrate spectrum, showed higher activities on glucomannan than on galactomannan, and released mannobiose and mannotriose as the main hydrolysis products after an extended incubation. Compared to the only functionally characterized and structure-resolved counterpart Alicyclobacillus acidocaldarius ManA (AaManA) of GH 113, Man113A showed much higher catalytic efficiency on mannooligosaccharides, in the order mannohexaose Ϸ mannopentaose > mannotetraose > mannotriose, and required at least four sugar units for efficient catalysis. Homology modeling, molecular docking analysis, and site-directed mutagenesis revealed the vital roles of eight residues (Trp13, Asn90, Trp96, Arg97, Tyr196, Trp274, Tyr292, and Cys143) related to substrate recognition by and catalytic mechanism of GH 113. Comparison of the binding pockets and key residues of ␤-mannanases of different families indicated that members of GH 113 and GH 5 have more residues serving as stacking platforms to support ؊4 to ؊1 subsites than those of GH 26 and that the residues preceding the acid/base catalyst are quite different. Taken as a whole, this study elucidates substrate recognition by and the catalytic mechanism of GH 113 ␤-mannanases and distinguishes them from counterparts of other families.A major component of hemicellulose in the plant cell walls of softwood, plant seeds, and beans is ␤-1,4-mannan, including mannan polysaccharides, glucomannan, galactomannan, and galactoglucomannan. It is composed of a backbone of ␤-1,4-linked mannose or a combination of glucose and mannose with side chains of ␣-1,6-linked galactose residues (1). The mannan-degrading enzymes have biotechnological applications in various areas, such as feed manufacturing (2), paper processing (3), and coffee extract treatment (4). Mannooligosaccharides, the major hydrolysis products of mannan, are beneficial as animal nutrition additives due to their potential prebiotic properties (5). The complete degradation of mannan polysaccharides into monomers requires an enzyme system including ␤-mannanase (EC 3.2.1.78), ␤-mannosidase (EC 3.2.1.25), ␤-glucosidase (EC 3.2.1.21), and ␣-galactosidase (EC 3.2.1.22). Of these, ␤-mannanase randomly hydrolyzes the ␤-D-1,4-mannopyranoside linkages and plays the major role in mannan degradation.␤-Mannanases are widely distributed in various organisms, including bacteria, yeasts, filamentous fungi, and plants. Based on the amino acid sequence and structural similarities of catalytic domains, ␤-mannanases are grouped into three glycoside hydrolase (GH) families in the Carbohydrate-Active enZYmes (CAZy) database (6), i.e., 5, 26, and 113. GH 1...

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“…Additional enzymes such as acetyl mannan esterase and α-galactosidase are important for the removal of side chain groups of mannan [6]. Based on the primary structures of their catalytic domains, β-mannanases are found in the glycoside hydrolase families 5, 26, and 113 [4,7,8]. These enzyme families present a double-displacement mechanism with retention of anomeric configuration.…”

Section: Introductionmentioning

confidence: 99%

“…According to Zhang and Sang [10], the filamentous fungi strains are the most interesting producers by right of higher yields of extracellular enzymes and association with cellulases production. Thermostable β-mannanases have great advantages, such as reducing the risk of contamination, increasing the substrate solubility, and improving the mass transfer rate [8,10].…”

Section: Introductionmentioning

confidence: 99%

Partial Purification and Characterization of a Thermostable β-Mannanase from Aspergillus foetidus

et al. 2015

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An extracellular β-mannanase was isolated from samples of crude extract of the mesophilic fungus Aspergillus foetidus grown on soybean husk as a carbon source. The induction profile showed that β-mannanase reached a maximum activity level (2.0 IU/mL) on the 15th day of cultivation. The enzyme was partially purified by ultrafiltration and gel filtration chromatography procedures and was named Man 58. Sodium dodecyl sulfate-polyacrilamide electrophoresis and zymogram analysis of Man 58 showed two bands of approximately 43 and 45 kDa with β-mannanase activity. Ultrafiltration showed that β-mannanase activity was only detected in the concentrated sample. Man 58 was most active at 60 °C and at pH 4.0. It was thermostable in the temperature range of 40-60 °C for eleven days, and the half-life at 70 °C was ten days. Man 58 showed Km and Vmax values of 3.29 mg/mL and 1.76 IU/mL respectively, with locust bean gum as a substrate. It was mostly activated by FeSO4 and CoCl2 and inhibited by MgSO4, FeCl3, CuSO4, MgCl2, ZnCl2, ZnSO4, CaCl2, CuCl2, KCl and ethylenediaminetetraacetic acid (EDTA). Phenolic compounds did not inhibit the OPEN ACCESSAppl. Sci. 2015, 5 882 enzyme. On the other hand, auto-hydrolysis liquor showed an inhibitory effect on Man 58 activity.

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

Cited by 58 publications

References 32 publications

Experimental design of response surface methodology used for utilisation of palm kernel cake as solid substrate for optimised production of fungal mannanase

Experimental design of response surface methodology used for utilisation of palm kernel cake as solid substrate for optimised production of fungal mannanase

A Novel Glycoside Hydrolase Family 113 Endo-β-1,4-Mannanase from Alicyclobacillus sp. Strain A4 and Insight into the Substrate Recognition and Catalytic Mechanism of This Family

Partial Purification and Characterization of a Thermostable β-Mannanase from Aspergillus foetidus

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