Purification and characterization of β-Mannanase from <i>Reinekea</i> sp. KIT-YO10 with transglycosylation activity

Hakamada, Yoshihiro; Ohkubo, Y.; Ohashi, Satoshi

doi:10.1080/09168451.2014.895658

Cited by 18 publications

(17 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The major products liberated from LBG were oligosaccharide with degree of polymerisation of 3 & 4. 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.…”

Section: Resultssupporting

confidence: 92%

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

View full text Add to dashboard Cite

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.

show abstract

Section: Resultssupporting

confidence: 92%

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

View full text Add to dashboard Cite

show abstract

“…2, D273, the acid/base proton donor) (Kumagai et al 2011). Whereas bacterial β-mannanases mainly belong to the GH5 and GH113 families (Fusco et al 2018;Zang et al 2015), the more acid-tolerant and catalytic efficient fungal β-mannanases are grouped into the GH5 and GH26 families (Do et al 2009;Hakamada et al 2014;Harnpicharnchai et al 2016;Katsimpouras et al 2016;Liao et al 2014;Naganagouda et al 2009;Wang et al 2015;Yu et al 2015) (Table 2). More recently, the identification of Man134A, produced by the filamentous fungus Aspergillus nidulans, led to the establishment of the new family of GH134 in the CAZy database (Shimizu et al 2015).…”

Section: β-Mannanasesmentioning

confidence: 99%

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Aulitto

Fusco

Limauro

et al. 2019

World J Microbiol Biotechnol

View full text Add to dashboard Cite

Extremophilic microorganisms are valuable sources of enzymes for various industrial applications. In fact, given their optimal catalytic activity and operational stability under harsh physical and chemical conditions, they represent a suitable alternative to their mesophilic counterparts. For instance, extremophilic enzymes are important to foster the switch from fossil-based to lignocellulose-based industrial processes. Indeed, more stable enzymes are needed, because the conversion of the lignocellulosic biomass to a wide palette of value-added products requires extreme chemo-physical pre-treatments. Galactomannans are part of the hemicellulose fraction in lignocellulosic biomass. They are heteropolymers constituted by a β-1,4-linked mannan backbone substituted with side chains of α-1,6-linked galactose residues. Therefore, the joint action of different hydrolytic enzymes (i.e. β-mannanase, β-mannosidase and α-galactosidase) is needed to accomplish their complete hydrolysis. So far, numerous galactomannan-degrading enzymes have been isolated and characterized from extremophilic microorganisms. Besides applications in biorefinery, these biocatalysts are also useful to improve the quality (i.e. digestibility and prebiotic properties) of food and feed as well as in paper industries to aid the pulp bleaching process. In this review, an overview about the structure, function and applications of galactomannans is provided. Moreover, a survey of (hyper)-thermophilic galactomannans-degrading enzymes, mainly characterized in the last decade, has been carried out. These extremozymes are described in the light of their biotechnological application in industrial processes requiring harsh conditions.

show abstract

“…Although multiple β -mannanase-producing bacteria have been reported [15, 16], they are far from the diverse industry needs. Currently, acidic and alkaline β -mannanase has been proposed to meet the industrial demands [17].…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Thermostableβ-Mannanase fromBacillus subtilisBE-91: Potential Application in Inflammatory Diseases

Cheng

Duan

Feng

et al. 2016

BioMed Research International

View full text Add to dashboard Cite

β-mannanase has shown compelling biological functions because of its regulatory roles in metabolism, inflammation, and oxidation. This study separated and purified the β-mannanase from Bacillus subtilis BE-91, which is a powerful hemicellulose-degrading bacterium using a “two-step” method comprising ultrafiltration and gel chromatography. The purified β-mannanase (about 28.2 kDa) showed high specific activity (79, 859.2 IU/mg). The optimum temperature and pH were 65°C and 6.0, respectively. Moreover, the enzyme was highly stable at temperatures up to 70°C and pH 4.5–7.0. The β-mannanase activity was significantly enhanced in the presence of Mn2+, Cu2+, Zn2+, Ca2+, Mg2+, and Al3+ and strongly inhibited by Ba2+ and Pb2+. K m and V max values for locust bean gum were 7.14 mg/mL and 107.5 μmol/min/mL versus 1.749 mg/mL and 33.45 µmol/min/mL for Konjac glucomannan, respectively. Therefore, β-mannanase purified by this work shows stability at high temperatures and in weakly acidic or neutral environments. Based on such data, the β-mannanase will have potential applications as a dietary supplement in treatment of inflammatory processes.

show abstract

Purification and characterization of β-Mannanase from Reinekea sp. KIT-YO10 with transglycosylation activity

Cited by 18 publications

References 35 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

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Purification and Characterization of a Thermostableβ-Mannanase fromBacillus subtilisBE-91: Potential Application in Inflammatory Diseases

Contact Info

Product

Resources

About