Abstract:A thermotolerant bacterium Paenibacillus thiaminolyticus with an ability to produce extracellular β-mannanase was isolated from a soil sample. Bacterium produced 45 U/mL β-mannanase at 50 °C. The culture conditions for high-level production of β-mannanase were optimized. Optimized MS medium [wheat bran 2% (w/v), ammonium sulfate 0.3% (w/v), yeast extract, and peptone (0.025% each) pH 6.5] was inoculated with 2% of 16 H old culture. The culture was incubated at 50 °C for 48 H resulting in 24-folds higher β-man… Show more
“…MOS are able to interfere in bacterial attachment (of Salmonella and E. coli ). In the intestinal tract, however, these oligosaccharides selectively promote the growth of beneficial bacteria, especially Lactobacillus and Bifidobacterium (Chauhan et al 2014 ; Dhawan et al 2015 ). Thus, the production of oligosaccharides with DP 3–4 makes A. terreus β-mannanase a good candidate for potential application in the feed industry.…”
Aspergillus terreus FBCC 1369 was grown in solid-state culture under statistically optimized conditions. b-Mannanase was purified to apparent homogeneity by ultrafiltration, anion exchange and gel filtration chromatography. A purification factor of 10.3-fold was achieved, with the purified enzyme exhibiting specific activity of 53 U/mg protein. The purified b-mannanase was optimally active at pH 7.0 and 70°C and displayed stability over a broad pH range of 4.0-8.0 and a 30 min halflife at 80°C. The molecular weight of b-mannanase was calculated as *49 kDa by SDS-PAGE. The enzyme exhibited K m and V max values of 5.9 mg/ml and 39.42 lmol/ml/min, respectively. b-Mannanase activity was stimulated by b-mercaptoethanol and strongly inhibited by Hg 2? . The b-Mannanase did not hydrolyze mannobiose and mannotriose, but only mannotetraose liberating mannose and mannotriose. This indicated that at least four mannose residues were required for catalytic activity. Oligosaccharide with a degree of polymerization (DP) three was the predominant product in the case of locust bean gum (16.5 %) and guar gum (15.8 %) hydrolysis. However, the enzyme liberated DP4 oligosaccharide (24 %) exclusively from konjac gum. This property can be exploited in oligosaccharides production with DP 3-4. b-Mannanase hydrolyzed pretreated lignocelluloses and liberated reducing sugars (% theoretical yield) from copra meal (30 %). This property is an important factor for the bioconversion of the biomass.
“…MOS are able to interfere in bacterial attachment (of Salmonella and E. coli ). In the intestinal tract, however, these oligosaccharides selectively promote the growth of beneficial bacteria, especially Lactobacillus and Bifidobacterium (Chauhan et al 2014 ; Dhawan et al 2015 ). Thus, the production of oligosaccharides with DP 3–4 makes A. terreus β-mannanase a good candidate for potential application in the feed industry.…”
Aspergillus terreus FBCC 1369 was grown in solid-state culture under statistically optimized conditions. b-Mannanase was purified to apparent homogeneity by ultrafiltration, anion exchange and gel filtration chromatography. A purification factor of 10.3-fold was achieved, with the purified enzyme exhibiting specific activity of 53 U/mg protein. The purified b-mannanase was optimally active at pH 7.0 and 70°C and displayed stability over a broad pH range of 4.0-8.0 and a 30 min halflife at 80°C. The molecular weight of b-mannanase was calculated as *49 kDa by SDS-PAGE. The enzyme exhibited K m and V max values of 5.9 mg/ml and 39.42 lmol/ml/min, respectively. b-Mannanase activity was stimulated by b-mercaptoethanol and strongly inhibited by Hg 2? . The b-Mannanase did not hydrolyze mannobiose and mannotriose, but only mannotetraose liberating mannose and mannotriose. This indicated that at least four mannose residues were required for catalytic activity. Oligosaccharide with a degree of polymerization (DP) three was the predominant product in the case of locust bean gum (16.5 %) and guar gum (15.8 %) hydrolysis. However, the enzyme liberated DP4 oligosaccharide (24 %) exclusively from konjac gum. This property can be exploited in oligosaccharides production with DP 3-4. b-Mannanase hydrolyzed pretreated lignocelluloses and liberated reducing sugars (% theoretical yield) from copra meal (30 %). This property is an important factor for the bioconversion of the biomass.
“…β-mannanase is extensively used in the paper/pulp, food, and feed industries, particularly in poultry feeds and prebiotic food supplements to decrease the immunogenic effect of mannan polymers, clarify fruit juices, and extract of oil from copra and detergent (Kaira et al, 2016;Singh et al, 2019). In these industries, thermostable enzymes are preferentially used (Dhawan et al, 2016;Li and Nie, 2016) due to their robustness and enhanced rate of hydrolysis (Katsimpouras et al, 2016;Niu et al, 2017). Moreover, thermozymes offer unique features such as high pH, solvent concentrations (Liu et al, 2019), and resistance to chemical denaturation (Akram et al, 2018), and they could reduce contamination from unwanted microbes (Ebaid et al, 2019).…”
Thermotoga maritima (Tma) contains genes encoding various hyperthermophilic enzymes with great potential for industrial applications. The gene TM1752 in Tma genome has been annotated as cellulase gene encoding protein Cel5B. In this work, the gene TM1752 was cloned and expressed in Escherichia coli, and the recombinant enzyme was purified and characterized. Interestingly, the purified enzyme exhibited specific activities of 416 and 215 U/mg on substrates galactomannan and carboxy methyl cellulose, which is the highest among thermophilic mannanases. However, the putative enzyme did not show sequence homology with any of the previously reported mannanases; therefore, the enzyme Cel5B was identified as bifunctional mannanase and cellulase and renamed as Man/Cel5B. Man/Cel5B exhibited maximum activity at 85°C and pH 5.5. This enzyme retained more than 50% activity after 5 h of incubation at 85°C, and retained up to 80% activity after incubated for 1 h at pH 5–8. The Km and Vmax of Man/Cel5B were observed to be 4.5 mg/mL galactomannan and 769 U/mg, respectively. Thin layer chromatography depicted that locust bean gum could be efficiently degraded to mannobiose, mannotriose, and mannooligosaccharides by Man/Cel5B. These characteristics suggest that Man/Cel5B has attractive applications for future food, feed, and biofuel industries.
“…Mannose-free manno-oligosaccharides (MOS) are desirable as prebiotics in nutraceutical industries. Recently, Chauhan et al (2014) and Dhawan et al (2015) have demonstrated the role of MOS as prebiotic in supporting growth of probiotics ( Lactobacillus and Bifidobacterium ) and inhibiting the growth of pathogen ( Salmonella enterica ). The focus of this study is the optimised production of β-mannanase on a solid substrate (PKC), a by-product of palm oil industry, and enzymatic hydrolysis of mannan (locust bean gum and konjac gum) for the generation of MOS.…”
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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