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1.
Indian J Exp Biol ; 2018 Jul; 56(7): 493-497
Article | IMSEAR | ID: sea-190962

ABSTRACT

Agricultural crop residues serve as a renewable source for production of bioethanol and other value added chemicals. Optimization of enzymatic saccharification may ensure cost-effective production of bioethanol and other industrially important products. Here, we attempted optimization of various process variables affecting enzymatic hydrolysis of microwave-assisted acid pretreated chili post-harvest residue was evaluated by adopting statistical design experiments. The optimum conditions of enzymatic hydrolysis were solid loading of 15% (w/w), cellulase loading of 20 FPU per gram of pretreated biomass and incubation time of 12 h. The high solid loading, low cellulase loading and low incubation time may lead to better process economics. Maximum reducing sugar yield of 0.205 g/g was observed. Fermentation inhibitors, such as furfural and 5-hydroxymethylfurfural were absent in the hydrolysate obtained after enzymatic saccharification of pretreated biomass and were found suitable for the production of various value added products like xylanases, bioethanol and biopolymer (poly-3-hydroxybutyrate).

2.
Indian J Exp Biol ; 2015 Jun; 53(6): 356-363
Article in English | IMSEAR | ID: sea-158505

ABSTRACT

Here, we described the production of a cellulase-free alkaline xylanase from Bacillus pumilus MTCC 5015 by submerged fermentation and its application in biobleaching. Various process parameters affecting xylanase production by B. pumilus were optimized by adopting a Plackett-Burman design (PBD) as well as Response surface methodology (RSM). These statistical methods aid in improving the enzyme yield by analysing the individual crucial components of the medium. Maximum production was obtained with 4% yeast extract, 0.08% magnesium sulphate, 30 h of inoculum age, incubation temperature of 33.5 °C and pH 9.0. Under optimized conditions, the xylanase activity was 372 IU/ml. Media engineering improved a 5-fold increase in the enzyme production. Scanning electron microscopy (SEM) showed significant changes on the surface of xylanase treated pulps as a result of xylan hydrolysis. Increased roughness of paper carton fibres was apparent in scanning electron micrograph due to opening of the micro fibrils present on the surface by xylanase action. The untreated pulp did not show any such change. These results demonstrated that the B. pumilus MTCC 5015 xylanase was effective in bio-bleaching of paper carton.


Subject(s)
Bacillus/chemistry , Bacillus/classification , Biotechnology , Cellulose/metabolism , Fermentation , Paper , Xylosidases/biosynthesis , Xylosidases/chemical synthesis
3.
Indian J Exp Biol ; 2013 Nov; 51(11): 875-884
Article in English | IMSEAR | ID: sea-149393

ABSTRACT

Xylanases are a group of depolymerizing enzymes often used for the hydrolysis of xylan (present in hemicellulose) to monomeric sugars and comprise endo-xylanases (EC 3.2.1.8) and β-xylosidases (EC 3.2.1.37). They often act in synergy with other enzymes for complete hydrolysis of hemicellulose. Xylanases find several industrial applications, for example in food and feed industries, paper and pulp industries and more recently have acquired a great role in biomass to biofuels program. Bacteria and fungi can best produce xylanases. Recent developments in rDNA technology have resulted in molecular cloning and expression of xylanases in heterologous and homologous hosts. In view of significance of the actinomycetes for the production of biotechnological products, attempts have been made in recent years to explore them for the production of industrial enzymes, including xylanses, aiming to find the enzyme with novel features. This review provides the state-of-art information and developments on the xylanases from actinomycetes, presenting the production, purification, characterization and over-expression from various actinomycetes cultures.


Subject(s)
Actinobacteria/enzymology , Endo-1,4-beta Xylanases/biosynthesis , Endo-1,4-beta Xylanases/isolation & purification , Endo-1,4-beta Xylanases/metabolism
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