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Kanjanavas, F; Khawsak, Paisarn; Pakpitcharoen, Arda; Areekit, Supatra; Sriyaphai, T; Pothivejkul, Khajeenart; Santiwatanakul, Somchai; Matsui, Kazuaki; Kajiwara, Tadahiko; Chansiri, Kosum

doi:10.2306/scienceasia1513-1874.2009.35.017

Cited by 13 publications

(3 citation statements)

References 23 publications

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“…(2) CcMan5C showed an optimal temperature of 70 °C for hydrolytic activity and retained over 80% of its activity after 1 h of incubation at 50 °C. Microbial mannanases have been shown to work at different temperatures, ranging from 37 °C to 70 °C [ 23 , 24 , 25 , 31 , 32 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 ]. Several bacterial mannanases have displayed thermostable properties, rising up to 93 °C [ 23 , 24 , 25 ].…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, CcMan5C tolerated detergents such as Tween 20 and Triton X-100, and its activity was even enhanced to 26.2–45.6% by 1% or 10% Tween 20 and Triton X-100. However, most microbial β-mannanases showed a reduction to a certain extent in activity by adding organic solvents such as methanol, ethanol, and acetone [ 6 , 48 , 50 , 51 ], except for an endo-1,4-β-mannonase from Bacillus pumilus GBSW19 that showed enhancing activity by adding low concentrations of 10% isopropanol and acetone, as well as 20% ethanol [ 47 ]. Some microbial β-mannanases showed an inhibition in activity by the addition of detergents such as SDS, Tween-20 and Triton X-100 [ 6 , 50 ], while others showed resistance to these detergents and even an increase in activity by the addition of SDS [ 32 , 52 ].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Heterologous Expression, Purification and Characterization of an Alkalic Thermophilic β-Mannanase CcMan5C from Coprinopsis cinerea

Yan

Duan

Liu

et al. 2023

JoF

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A endo-1,4-β-mannanase (CcMan5C) gene was cloned from Coprinopsis cinerea and heterologously expressed in Pichia pastoris, and the recombinant enzyme was purified by Ni-affinity chromatography and identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF-MS). CcMan5C hydrolyzed only locust bean gum galactomannan (LBG) but not α-mannan from S. cerevisiae or Avicel cellulose, oat spelt xylan, or laminarin from Laminaria digitata. CcMan5C exhibited distinctive catalytic features that were different from previously reported β-mannanases. (1) CcMan5C is the first reported fungal β-mannase with an optimal alkalic pH of 8.0–9.0 for hydrolytic activity under assay conditions. (2) CcMan5C is the first reported alkalic fungal β-mannase with an optimal temperature of 70 °C for hydrolytic activity under assay conditions. (3) The organic solvents methanol, ethanol, isopropanol, and acetone at concentrations of 10% or 20% did not inhibit CcMan5C activity, while 10% or 20% isopropanol and acetone even enhanced CcMan5C activity by 9.20–34.98%. Furthermore, CcMan5C tolerated detergents such as Tween 20 and Triton X-100, and its activity was even enhanced to 26.2–45.6% by 1% or 10% Tween 20 and Triton X-100. (4) CcMan5C solution or lyophilized CcMan5C exhibited unchanged activity and even increasing activity after being stored at −20 °C or −80 °C for 12 months and retained above 50% activity after being stored at 4 °C for 12 months. These features make CcMan5C a suitable candidate for the detergent industry and paper and pulp industry.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Heterologous Expression, Purification and Characterization of an Alkalic Thermophilic β-Mannanase CcMan5C from Coprinopsis cinerea

Yan

Duan

Liu

et al. 2023

JoF

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“…For instance, β-mannanases (GH 26) from Bacillus sp. CFR1601 [57], Bacillus subtilis BCC41051 [58], Bacillus licheniformis [59] and Bacillus subtilis B23 [20] are optimally active at pH 7. β-mannanases (GH 26) from Bacillus N16-5 (GH 26) [60], Bacillus licheniformis THCM 3.1 [61] and Bacillus sp. strain JAMB-750 [62] are optimally active at pH 9.6, 9.0 and 10.0, respectively.…”

Section: Discussionmentioning

confidence: 99%

Expression, Characterization and Structure Analysis of a New GH26 Endo-β-1, 4-Mannanase (Man26E) from Enterobacter aerogenes B19

Liu

Cui

2020

Applied Sciences

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β-mannanase is one of the key enzymes to hydrolyze hemicellulose. At present, most β-mannanases are not widely applied because of their low enzyme activity and unsuitable enzymatic properties. In this work, a new β-mannanase from Enterobacter aerogenes was studied, which laid the foundation for its further application. Additionally, we will further perform directed evolution of the enzyme to increase its activity, improve its temperature and pH properties to allow it more applications in industry. A new β-mannanase (Man26E) from Enterobacter aerogenes was successfully expressed in Escherichia coli. Man26E showed about 40 kDa on SDS-PAGE gel. The SWISS-MODEL program was used to model the tertiary structure of Man26E, which presented a core (α/β)8-barrel catalytic module. Based on the binding pattern of CjMan26 C, Man26E docking Gal1Man4 was investigated. The catalytic region consisted of a surface containing four solvent-exposed aromatic rings, many hydrophilic and charged residues. Man26E displayed the highest activity at pH 6.0 and 55 °C, and high acid and alkali stability in a wide pH range (pH 4–10) and thermostability from 40 to 50 °C. The enzyme showed the highest activity on locust bean gum, and the Km and Vmax were 7.16 mg mL−1 and 508 U mg−1, respectively. This is the second β-mannanase reported from Enterobacter aerogenes B19. The β-mannanase displayed high enzyme activity, a relatively high catalytic temperature and a broad range of catalytic pH values. The enzyme catalyzed both polysaccharides and manno-oligosaccharides.

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Purification and characterization of an alkali-thermostable β-mannanase from Bacillus nealsonii PN-11 and its application in mannooligosaccharides preparation having prebiotic potential

Chauhan

Sharma

Puri³

et al. 2014

Eur Food Res Technol

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Cited by 13 publications

References 23 publications

Heterologous Expression, Purification and Characterization of an Alkalic Thermophilic β-Mannanase CcMan5C from Coprinopsis cinerea

Heterologous Expression, Purification and Characterization of an Alkalic Thermophilic β-Mannanase CcMan5C from Coprinopsis cinerea

Expression, Characterization and Structure Analysis of a New GH26 Endo-β-1, 4-Mannanase (Man26E) from Enterobacter aerogenes B19

Purification and characterization of an alkali-thermostable β-mannanase from Bacillus nealsonii PN-11 and its application in mannooligosaccharides preparation having prebiotic potential

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