Characterization of β-mannanase extracted from a novel Streptomyces species Alg-S25 immobilized on chitosan nanoparticles

Figures & data

Table 1. Biotechnological applications of β-mannanase.

Industry	Potential application
Biorefinery	Facilitating efficient enzymatic degradation of lignocellulosic wastes into sustainable products [13,14].
Detergent	Applying as an additive for the effective removal of sticky gum stains from fabrics [20].
Fodder	Improving the palatability and digestibility of livestock feeds [21–24].
Food processing	Reducing the viscosity of coffee extract during the production of instant coffee [25]; extracting oil from coconut meat and palm kernel [26]; macerating and clarifying fruits and vegetables [20].
Oil and gas	Enhancing the recovery of oil and gas during the drilling process [27].
Pharmaceuticals	Using as a therapeutic agent for irritable bowel syndrome, acute diarrhea in children and as a prebiotic [14,20].
Pulp and paper	Inducing the biobleaching of paper and softwood pulp [27,28].
Textile	Reducing the viscosity of printing paste used in textile processing [29].
Waste water treatment	Controlling the slime and biofilm formations by inhibiting bacterial adhesion to the surfaces [20,28].

Figure 1. Phylogenetic affiliation of Streptomyces sp. Alg-S25 based on 16S rRNA gene sequences. The numbers at the nodes indicate the bootstrap percentage values of 1000 iterations. GenBank accession numbers are specified in the parentheses. Scale indicates 0.002 substitutions per nucleotide position.

Figure 2. FTIR spectra of glutaraldehyde-activated chitosan nanoparticles (a) and chitosan nanoparticle-immobilized β-mannanase (b).

Figure 3. Influence of pH on free and immobilized β-mannanase activity. Analyses were conducted three times and data are reported as mean values ± SD.

Figure 4. Influence of pH on free and immobilized β-mannanase stability. Analyses were conducted three times and data are reported as mean values ± SD.

Figure 5. Influence of temperature on free and immobilized β-mannanase activity. Analyses were conducted three times and data is reported as mean values. Standard deviations are less than 5% of mean values. Error bars are not displayed for the clarity.

Figure 6. Influence of temperature on free and immobilized β-mannanase stability. Analyses were conducted three times and data are reported as mean values ± SD.

Figure 7. Effect of sodium chloride on free and immobilized β-mannanase activity. Analyses were conducted three times and data are reported as mean values ± SD.

Table 2. Influence of metal ions and inhibitors on free and nanoparticle-immobilized β-mannanase activity.

Metal ions and inhibitors	Free		Immobilized
	% activity retained
	0.1 mmol/L	1 mmol/L	0.1 mmol/L	1 mmol/L
Ca^2+	126.0 ± 5.89	109.0 ± 4.82	144.0 ± 6.54	114.0 ± 5.23
Cu^2+	46.3 ± 1.98	28.1 ± 1.21	51.6 ± 2.29	36.2 ± 1.59
Mg^2+	130.0 ± 5.32	116.0 ± 4.65	152.0 ± 7.12	131.0 ± 6.21
Mn^2+	31.8 ± 1.23	23.6 ± 0.87	36.3 ± 1.21	24.3 ± 1.12
Ni^2+	52.6 ± 1.18	30.5 ± 1.43	56.1 ± 2.64	33.8 ± 1.42
DTT	96.4 ± 4.23	94.1 ± 4.13	98.3 ± 4.63	97.1 ± 4.54
EDTA	28.3 ± 1.29	15.1 ± 0.55	30.4 ± 1.13	20.2 ± 0.87
Iodoacetic acid	29.7 ± 1.16	17.1 ± 0.76	29.9 ± 1.38	19.3 ± 0.81
PMSF	30.1 ± 1.12	11.2 ± 0.48	31.6 ± 1.43	13.4 ± 0.55

DTT: dithiothreitol; PMSF: phenylmethanesulfonyl fluoride.

Figure 8. Repetitive application of nanoparticle immobilized β-mannanase. Analyses were conducted three times and the values of residual specific activity are reported as mean values ± SD.

Van Dyk JS, Pletschke BI. A review of lignocellulose bioconversion using enzymatic hydrolysis and synergistic cooperation between enzymes-factors affecting enzymes, conversion and synergy. Biotechnol Adv. 2012;30(6):1458–1480.

 PubMed Web of Science ®Google Scholar

Yamabhai M, Ubol SS, Srila W, et al. Mannan biotechnology: from biofuels to health. Crit Rev Biotechnol. 2016;36(1):32–42.

 PubMed Web of Science ®Google Scholar

Chauhan PS, Puri N, Sharma P, et al. Mannanases: microbial sources, production, properties and potential biotechnological applications. Appl Microbiol Biotechnol. 2012;93(5):1817–1830.

 PubMed Web of Science ®Google Scholar

Sachslehner A, Foidl G, Foidl N, et al. Hydrolysis of isolated coffee mannan and coffee extract by mannanases of Sclerotium rolfsii. J Biotechnol. 2000;80(2):127–134.

 PubMed Web of Science ®Google Scholar

Jørgensen H, Sanadi AR, Felby C, et al. Production of ethanol and feed by high dry matter hydrolysis and fermentation of palm kernel press cake. Appl Biochem Biotechnol. 2010;161(1–8):318–332.

 PubMed Web of Science ®Google Scholar

Gübitz GM, Sachslehner A, Haltrich D. Microbial mannanases: substrates, production, and applications. In: Himmel ME, Baker JO, Saddler JN, editors. Glycosyl hydrolases for biomass conversion. ACS Symposium Series, Vol. 769. Washington, (DC): American Chemical Society; 2000. p. 236–262.

 Google Scholar

Dhawan S, Kaur J. Microbial mannanases: an overview of production and applications. Crit Rev Biotechnol. 2007;27(4):197–216.

 PubMed Web of Science ®Google Scholar

Ademark P, Varga A, Medve J, et al. Softwood hemicelluloses-degrading enzymes from Aspergillus niger: purification and properties of a β-mannanase. J Biotechnol. 1998;63(3):199–210.

 PubMed Web of Science ®Google Scholar