Cost-effective scouring of flax fibers using cellulase-free xylano-pectinolytic synergism from a bacterial isolate

et al. 2019

Biotechnology Progress

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This study shows the presence of five isozymic forms of alkaline xylanase from Bacillus pumilus using fast flow rate microfiltration, ultrafiltration, Q-sepharose, and phenyl sepharose chromatographic techniques. Polyacrylamide gel electrophoresis, highperformance liquid chromatography, and zymographic studies also revealed the purity of five isoforms of alkaline xylanases. Isoforms-X-I, X-III, and X-V exhibited optimum activity at pH 8.5, whereas X-II, X-IV showed maximum activity at pH 9. All isoforms were optimally active at temperature 55 C. Isoforms were found to be stable at pH 7-11, showed 92-100% residual activity after 3 hr, treatment time for most industrial applications. The isoforms retained nearly 80-86% residual activity after incubating at 45 C for 3 hr. Molecular weights of xylanase I-V, were 13.1, 15.3, 18.4, 20.1, and 21.0 kDa, respectively. Mg 2+ ions were found to be potent activator for all isozymic forms. The Km and Vmax values of X-I, X-II, X-III, X-IV, and X-V were 6.71, 6.66, 7.14, 5.88, 6.25 mg/ml and 2,000, 1,695, 1,666.66, 1,428.57, and 1,408.45 IU/mg protein, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed the monomeric nature of all isoforms. The lowmolecular masses, significantly enhanced activity in the presence of industrially suitable-low cost activator, better stability of all isoforms at pH 7-11 and at higher temperature, also presence of multiple forms of alkaline xylanase, makes this enzyme suitable for textile-paper industries. This is also the first report mentioning the purification of five isozymic forms of alkaline xylanase using fast flow rate techniques.

Section: Introductionmentioning

confidence: 99%

Fast flow rate processes for purification of alkaline xylanase isoforms from Bacillus pumilus AJK and their biochemical characterization for industrial application purposes

Singh

Sharma

et al. 2019

Biotechnology Progress

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“…Xylanases and pectinases are the two most valuable enzymes of commercial sector holding biotechnological significance and are being exploited since last decade due to their tremendous applicability in a spectrum of industrial processes, viz bleaching in paper and pulp industry, textile industry, recycling of paper, extraction and clarification of various fruit juices, etc. Production of xylanase and pectinase individually from different types of microorganisms has been reported by several researchers but only few reports are available till date mentioning their synthesis in combination, from a single microbial isolate …”

Section: Introductionmentioning

confidence: 99%

A novel and cost‐effective methodology for enhanced production of industrially valuable alkaline xylano‐pectinolytic enzymes cocktail in short solid‐state fermentation cycle

Agrawal

Mahajan

2019

Biotechnology Progress

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The aim of this study was to enhance the production of xylano‐pectinolytic enzymes concurrently and also to reduce the fermentation period. In this study, the effect of agro‐residues extract‐based inoculum on yield and fermentation time of xylano‐pectinolytic enzymes was studied. Microbial inoculum and fermentation media were supplemented with xylan and pectin polysaccharides derived from agro‐based residues. Enzymes production parameters were optimized through two‐stage statistical design approach. Under optimized conditions (temperature 37°C, pH 7.2, K2HPO4 0.22%, MgSO4 0.1%, gram flour 5.6%, substrate: moisture ratio 1:2, inoculum size 20%, agro‐based crude xylan in production media 0.45%, and agro‐based crude xylan–pectin in inoculum 0.13%), nearly 28,255 ± 565 and 9,202 ± 193 IU of xylanase and pectinase, respectively, were obtained per gram of substrate in a time interval of 6 days only. The yield of both xylano‐pectinolytic enzymes was enhanced along with a reduction of nearly 24 h in fermentation time in comparison with control, using polysaccharides extracted from agro‐residues. The activity of different types of pectinase enzymes such as exo‐polymethylgalacturonase (exo‐PMG), endo‐PMG, exo‐polygalacturonase (exo‐PG), endo‐PG, pectin lyase, pectate lyase, and pectin esterase was obtained as 1,601, 12.13, 5637, 24.86, 118.62, 124.32, and 12.56 IU/g, respectively, and was nearly twofold higher than obtained for all seven types in control samples. This is the first report mentioning the methodology for enhanced production of xylano‐pectinolytic enzymes in short solid‐state fermentation cycle using agro‐residues extract‐based inoculum and production media.

“…Few reports are available on the production of xylanases and pectinases under SSF by bacterial systems . Xylanses and pectinases are being used for various industrial applications such as recycling of waste paper , bleaching of paper pulp , and scouring of plant fibers . But there are only two reports available till date from fungi regarding the simultaneous production of xylanase and pectinase under SSF, that is, from Aspergillus awamori and Aspergillus niger F3 .…”

Section: Introductionmentioning

confidence: 99%

Simultaneous production of industrially important alkaline xylanase‐pectinase enzymes by a bacterium at low cost under solid‐state fermentation conditions

Kaur

Biotech and App Biochem

Mahajan

2019

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Simultaneous production of alkaline xylanase and all seven types of pectinases by a bacterial isolate, under solid-state fermentation was checked in this study. Under optimized conditions, high concurrent production of xylanase (22,800 ± 578 IU/g substrate) and pectinase (4,832 ± 189 IU/g substrate) was achieved. The different types of pectinases produced were exo-polymethylgalacturonase (782 IU/g), endo-polymethylgalacturonase (6.42 U/g), exo-polygalacturonase (2,250 IU/g), endo-polygalacturonase (11.57 U/g), polymethylgalacturonate lyase (53.99 IU/g), polygalacturonate lyase (59.78 IU/g), and pectin esterase (5.78 IU/g). Wheat bran resulted in the highest titer of both enzymes. The maximum xylanase-pectinase yield was detected after 7 days of incubation with 2 mM MgSO 4 and 1.5 g/L K 2 HPO 4 at wheat bran to moisture ratio 1:1.5 (w/v), media to flask volume ratio 1:25, pH 7.0, temperature 37 • C, and inoculum size 15%. Xylanase was most stable at pH 8.0, retained more than 75% activity up to 24 H, whereas pectinase was most stable at pH 9.0, having full activity even after 24 H. At 45 • C, the xylanase showed 82% residual activity after 6 H of incubation. The pectinase was 97% and 61% stable up to 3 H at 50 and 55 • C, respectively. This is the first report showing the production of xylanase-pectinases by bacterium along with high titer of seven types of pectinases, suitable for industries.