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Biotechnological Modes of Xylooligosaccharides Production from Waste Biomass: An Economic and Ecological Approach
Published in Prakash K. Sarangi, Latika Bhatia, Biotechnology for Waste Biomass Utilization, 2023
Latika Bhatia, Khageshwari Karsh, Suman Sahu, Dilip Kumar Sahu, Sonia Johri
Adoption of enzymatic degradation of xylan to produce XOS is economic and environment friendly when compared with physio-chemical processing methods (Dotsenko et al., 2017). Enzymes selectively attack the substrate, producing the desired product only. Xylanase is a class of enzymes that manifest the degradation of the linear polysaccharide ß-1, 4-Xylan into xylose. Xylanase is the extracellular product of bacteria, yeast, and filamentous fungi. Trichoderma, Aspergillus, Fusarium, and Pichia are a few fungal genera that are considered to be the potential producers of xylanases. Xylanases of microbial origin have significant utilization in xylan breakdown. Substrate xylan is a biopolymer made up of D-xylose monomers associated through ß1–4 glycozyl bond, which prevail profusely in lignocellulosic biomass. Xylanases can be classified as endo and exoxylanases. Exoxylanases (ß D-xylopyranosidase) are sometimes known as extracellular xylanase. There are three ways to classify Xylanases: based on the molecular weight and isoelectric point (pI), the structure of the crystal and kinetic properties, or the specificity of the substrate and product profile (Mane et al., 2018). Xylanases are inducible enzymes. In presence of xylan, the microorganism produces this enzyme in extracellular surroundings. Xylan is broken down and gets metabolized as a source of carbon. Xylan cannot enter the cell. Oligosaccharide is produced in this process (Mane et al., 2018).
Sequential optimization of xylanase production using Sapindus mukorossi seed waste in Lechevalieria aerocolonigenes
Published in Preparative Biochemistry & Biotechnology, 2022
Rohini Pawar, Shweta Pawar, Virendra Rathod
Since xylan is the second most abundant polymer, xylan degrading enzymes are produced by a variety of microbial species. Numerous literature is available for xylanase production using prokaryotes such as bacteria and cyanobacteria as well as eukaryotes such as yeast and fungi. The bacterial genera include Bacillus, Cellulomonas, Clostridium, and Arthrobacter, whereas Trichoderma, Aspergillus, and Penicillium constitute the fungal genera.[4] However, actinomycetes, a separate taxonomic group of bacteria, remained underexplored for the production of hydrolytic enzymes despite being very potent producers of lignocellulolytic enzymes. Limited data is available for the production of lignocellulolytic enzyme xylanase from actinomycetes Streptomyces[5] and Lechevalieria.[6] Since actinomycetes are inhabitants of terrestrial and aquatic environments, including extremophiles, the production study of industrially important hydrolytic enzymes is of great importance. Enzymes from saline environments and thermophilic regions will have tolerating capabilities of salt and temperature, which can help to establish environment-friendly processes using enzymes.[7]
Optimization of saccharification of enzymatically pretreated sugarcane tops by response surface methodology for ethanol production
Published in Biofuels, 2019
Knawang Chhunji Sherpa, Makarand Madhao Ghangrekar, Rintu Banerjee
Saccharification of lignocellulosics can be conducted with the help of a cocktail of enzymes that consists of cellulases and hemicellulases that work together [9]. Cellulases can be of three types, i.e. endoglucanase, exoglucanase and β-glucosidase. Cello-oligosaccharides are released when endoglucanase attacks the cellulose chains randomly; they are then acted on by exoglucanase which attacks the ends of cello-oligosaccharides to cellobiose. β-glucosidase then acts on the cellobiose to liberate glucose units. Xylanase on the other hand hydrolyses the xylan component of the biomass. Since pretreatment and saccharification are vital steps, its effectiveness generally determines the feasibility and ethanol yield in the fermentation step [10].
Lignocellulose derived functional oligosaccharides: production, properties, and health benefits
Published in Preparative Biochemistry and Biotechnology, 2019
Latika Bhatia, Ashutosh Sharma, Rakesh K. Bachheti, Anuj K. Chandel
Enzymatic processing appeals to be more economical, quick, and eco-friendly than physicochemical processing methods. Moreover, enzymatic processing neither generates harmful compounds nor requires special instrumentations.[33] Different enzymatic methods with the enzyme formulations have been applied for the extraction of galacto-oligosaccharides (Table 3). Dotsenko et al.[29] worked on monocotyledonous biomass, wheat straw, and ryegrass to produce linear XOS and branched arabinoxylooligosaccharides (AXOS) through enzymatic process. XOS is naturally available in fruits, vegetables, honey, and milk and can be produced at industrial scale. However, to meet the increasing demand, natural xylan-rich materials can be harnessed for XOS production. Xylanase is used in the production of XOS which have wide use as prebiotic and food additive in the food industry.[28] The pretreatment of hemicellulose is a pivotal step in the process of recovery of xylan from dried orange fruit wastes powder. Gupta et al.[37] used the waste of orange fruit to produce produced XOS. They reported that orange wastes are an excellent source of xylan which can be harnessed as a raw material for XOS production. Both chemical or enzymatic method can be approached for the same, but to minimize inhibitors production, enzymatic methods are given preference. They employed xylanase for this work. Enzymes with endo-xylanase activity are preferred over exo-xylanase activity so that the monosaccharide xylose production can be minimized thereby enhancing XOS production. There are many factors that govern the yield of XOS through enzymatic extraction. Prominent among them are a source of xylan, enzyme activity as well as incubation parameters such as the quantity of enzyme, pH, reaction time and temperature.[27] Hemicellulose is a heteropolymer that possesses a wide spectrum of chemical linkages. Hence, in order to hydrolyze it completely, the action of a larger repertoire of enzymes is required. These enzymes include endo-β-1,4-xylanases ([EC 3.2.1.8]), xylan 1,4-β-xylosidases ([EC 3.2.1.37]), α-L-arabinofuranosidases ([EC 3.2.1.55]), α-glucuronidases ([EC 3.2.1.139]), acetylxylanesterases ([EC 3.1.1.72]), feruloyl esterases ([EC 3.1.1.73]), mannan endo-1,4-β-mannanases ([EC 3.2.1.78]), β-1,4-mannosidases ([EC 3.2.1.25]), and arabinan endo-1,5-α-L-arabinosidases ([EC 3.2.1.99]).[25]