scholarly journals Isolation, Production, and Characterization of Thermotolerant Xylanase from Solvent TolerantBacillus vallismortisRSPP-15

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Rajeeva Gaur ◽  
Soni Tiwari ◽  
Priyanka Rai ◽  
Versha Srivastava
Keyword(s):  
Organic Solvent ◽  
Xylanase Activity ◽  
Industrial Applications ◽  
Birch Wood ◽  
Bacterial Strains ◽  
Xylanase Production ◽  
Birch Wood Xylan ◽  
Bacillus Vallismortis ◽  
Cu Ions

Sixty bacterial strains isolated from the soils sample in the presence of organic solvent were screened for xylanase production. Among them, strain RSPP-15 showed the highest xylanase activity which was identified asBacillus vallismortis. The isolate showed maximum xylanase production (3768 U/mL) in the presence of birch wood xylan and beef extract at 55°C pH 7.0 within 48 h of incubation. The enzyme activity and stability were increased 181.5, 153.7, 147.2, 133.6, and 127.9% and 138.2, 119.3, 113.9, 109, and 104.5% in the presence of Co2+, Ca2+, Mg+2, Zn+2, and Fe+3ions (10 mM). Xylanase activity and stability were strongly inhibited in the presence of Hg and Cu ions. The enzyme was also stable in the presence of 30% ofn-dodecane, isooctane,n-decane, xylene, toluene,n-hexane,n-butanol, and cyclohexane, respectively. The presence of benzene, methanol, and ethanol marginally reduced the xylanase stability, respectively. This isolate may be useful in several industrial applications owing to its thermotolerant and organic solvent resistance characteristics.

scholarly journals A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Abhay Raj ◽  
Sharad Kumar ◽  
Sudheer Kumar Singh
Keyword(s):  
Stenotrophomonas Maltophilia ◽  
Enzyme Stability ◽  
Xylanase Activity ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Exchange Chromatography ◽  
Rrna Gene ◽  
Bacterial Strains ◽  
Biochemical Tests ◽  
Xylanase Production

Seven xylanolytic bacterial strains were isolated from saw-dust dump soil. The bacterial strain X6 was selected on the basis of the highest xylanase activity with no cellulase contamination. It was identified as Stenotrophomonas maltophilia by biochemical tests and 16S rRNA gene sequencing approach. Xylanase production studies by S. maltophilia on different commercial xylans and agro-industrial residues suggested that wheat bran was the best carbon source for xylanase production (26.4 ± 0.6 IU/mL). The studies with inorganic and organic nitrogen sources suggested yeast extract as the best support for xylanase production (25 ± 0.6 IU/mL). Maximum xylanase production was observed at initial medium pH = 8.0 (23.8 ± 0.4 IU/mL) with production at pH = 7.0 and pH = 9.0 being almost comparable. Xylanase produced by S. maltophilia was purified to homogeneity using ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. The final purification was 5.43-fold with recovery of 19.18%. The molecular weight of the purified xylanase protein was ~142 kDa. Both crude and purified xylanase had good stability at pH = 9.0 and 80°C with activity retention greater than 90% after 30 min incubation. The enzyme stability at high temperature and alkaline pH make it potentially effective for industrial applications.

scholarly journals Production and Partial Characterization of an Alkaline Xylanase from a Novel FungusCladosporium oxysporum

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Guo-Qiang Guan ◽  
Peng-Xiang Zhao ◽  
Jin Zhao ◽  
Mei-Juan Wang ◽  
Shu-Hao Huo ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Wheat Bran ◽  
Internal Transcribed Spacer ◽  
Gene Sequence ◽  
Agricultural Waste ◽  
Xylanase Activity ◽  
Maximum Activity ◽  
Alkaline Proteases ◽  
Xylanase Production

A new fungusCladosporium oxysporumGQ-3 producing extracellular xylanase was isolated from decaying agricultural waste and identified based on the morphology and comparison of internal transcribed spacer (ITS) rDNA gene sequence.C. oxysporumproduced maximum xylanase activity of 55.92 U/mL with wheat bran as a substrate and NH4Cl as a nitrogen source. Mg2+improvedC. oxysporumxylanase production.Partially purified xylanase exhibited maximum activity at 50°C and pH 8.0, respectively, and showed the stable activity after 2-h treatment in pH 7.0–8.5 or below 55°C. Mg2+enhanced the xylanase activity by 2% while Cu2+had the highest inhibition ratio of 57.9%. Furthermore,C. oxysporumxylanase was resistant to most of tested neutral and alkaline proteases. Our findings indicated thatCladosporium oxysporumGQ-3 was a novel xylanase producer, which could be used in the textile processes or paper/feed industries.

scholarly journals Characterization of a NewProvidenciasp. Strain X1 Producing Multiple Xylanases on Wheat Bran

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Abhay Raj ◽  
Sharad Kumar ◽  
Sudheer Kumar Singh ◽  
Mahadeo Kumar
Keyword(s):  
Wheat Bran ◽  
Kraft Pulp ◽  
Enzyme Preparation ◽  
Xylanase Activity ◽  
Syringic Acid ◽  
Industrial Applications ◽  
Xylan Hydrolysis ◽  
Crude Enzyme Preparation ◽  
Crude Preparation

Providenciasp. strain X1 showing the highest xylanase activity among six bacterial isolates was isolated from saw-dust decomposing site. Strain X1 produced cellulase-free extracellular xylanase, which was higher in wheat bran medium than in xylan medium, when cultivated at pH 8.0 and 35°C. Zymogram analysis of crude preparation of enzymes obtained while growing on wheat bran and birchwood xylan revealed the presence of seven and two distinct xylanases with estimated molecular weight of 33; 35; 40; 48; 60; 75; and 95 kDa and 33 and 44 kDa, respectively. The crude xylanases were produced on wheat bran medium and showed optimum activity at pH 9.0 and 60°C. The thermotolerance studies showed activity retention of 100% and 85% at 40°C and 60°C after 30 min preincubation at pH 9.0. It was tolerant to lignin, ferulic acid, syringic acid, and guaiacol and retained 90% activity after ethanol treatment. The enzyme preparation was also tolerant to methanol and acetone and showed good activity retention in the presence of metal ions such as Fe2+, Mg2+, Zn2+, and Ca2+. The crude enzyme preparation was classified as endoxylanase based on the product pattern of xylan hydrolysis. Pretreatment of kraft pulp with crude xylanases for 3 h at 60°C led to a decrease in kappa number by 28.5%. The properties of present xylanases make them potentially useful for industrial applications.

scholarly journals Exploration of endo-xylanase from novel strain of Bacillus velezensis AG20 isolated from the cave of Meghalaya

2020 ◽  
Author(s):  
Arabinda Ghosh ◽  
Shravanika Mahanta ◽  
Subhro Banerjee ◽  
Debabrat Baishya
Keyword(s):  
Ecological Niche ◽  
Orthogonal Design ◽  
Bacterial Strains ◽  
Bacillus Velezensis ◽  
Xylanase Production ◽  
Cell Biomass ◽  
Prime Objective ◽  
Hydrolysis Of ◽  
Industrial Demand

ABSTRACTCave sets the example of extreme ecological niche and habitat for diversified microorganisms. Present study involved in the isolation of endoxylanase producing novel strain Bacillus velezensis AG20 from the Krem Phyllut cave, Meghalaya, India. Culture dependent studies, molecular phylogentics, RNA secondary folding pattern based on 16S rDNA substantiated the identity of this novel strain. Bacillus velezensis AG20 revealed the superbug quality having resistance against various class of broad-spectrum antibiotics. Bacillus velezensis AG20 revealed biofilm formation over the cell surface in FESEM. Highest cell biomass and xylanase production supported in TB medium, further purified partially to 5.3 fold with 21% yield. Molecular weight of the purified xylanase found to be 45 kDa. Enzyme kinetics and pattern of hydrolysis revealed the evidence for the selection of linear birchwood xylan with Vmax = 21.0 ± 3.0 U/ml, Km = 1.25 mg/ml, Kcat = 1.75/s at optimum pH 7 and temperature 50°C also found significant statistically in Taguchi’s orthogonal design. Conversely, ruled out any exoacting activity against synthetic pNP-xylopyranoside substrate. Endo-xylanase isolated from Bacillus velezensis AG20 was moderately thermostable over temperatures 50 and 60°C. Time dependent hydrolysis of agro-waste sugar cane bagasse depicted the production of xylooligosaccharides (XOS) predominantly xylobiose, xylotriose and xylotetrose. Purified mixed XOS hold their prebiotic potential by promoting the growth of probiotics Bifidobacterium and Lactobacillus as well as high stability (~90%) against systemic fluids. Mixed XOS (300 μg/ml) displayed anti-proliferation activities by reducing the growth of HT-29 and Caco-2 cells significantly 90% and 75%, respectively, after 48 h.IMPORTANCEExtremophiles dwelling inside the caves have laden with the extraordinary capabilities of bioconversion by nature. The pristine ecological niche inside the cave, absence of proper light and air, supports the livelihood of novel microorganisms. In India, Meghalaya is hoisting longest caves in the East Khasi Hills, providing conducive environment for novel bacterial strains. With the prime objective of isolating novel bacterial strains that produce extracellular xylanase our studies have been carried out. Considering the present industrial demand for nutraceutical, prebiotics, anti-proliferating agents and biofuels by the conversion of lignocellulosic biomass (LCB), novel enzymes are required. Xylanases from bacterial origin play a significant role in conversion of LCB into oligosaccharides. Therefore, exploration and characterization of xylanase producing novel isolate from cave may pave the new arena for the production of prebiotic and anti-inflammatory oligosaccharides from agro-waste.

Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23

1993 ◽  
Vol 39 (12) ◽  
pp. 1162-1166 ◽  
Author(s):  
A. Blanco ◽  
F. I. J. Pastor
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Xylanase Activity ◽  
Hydrolytic Activity ◽  
Bacillus Sp ◽  
Birchwood Xylan ◽  
Xylanase Production ◽  
Ph Values ◽  
Wide Range ◽  
Molecular Masses

A Bacillus strain with xylanase activity has been isolated. Maximum xylanase production was obtained when the strain was cultured in media supplemented with birchwood xylan or rice straw; production was repressed by glucose and xylose. The optimal temperature and pH for xylanase activity were 45–50 °C and 5.5–7.5, respectively. Crude xylanase was highly stable at a wide range of pH values, retaining 100% of the activity after 24 h of incubation at 37 °C in buffer at pH 10.0. Analysis by polyacrylamide gel electrophoresis and zymogram techniques showed four xylanase activity bands with apparent molecular masses of 32, 48, 61, and 66 kDa. The most active of them (molecular mass 32 kDa) apparently corresponded to a xylanase with an isoelectric point (pI) of 9.3 in isoelectrofocusing gels developed as zymograms. Four other bands with xylanase activity were detected at pIs of 7.7, 5.6, 5.0, and 4.5. Analysis for carboxymethylcellulase activity revealed that only the band of 48 kDa and the band with a pI of 7.7 showed hydrolytic activity against the cellulosic substrate.Key words: Bacillus sp., xylanase, isolation.

scholarly journals Production, Purification, and Characterization of a MajorPenicillium glabrumXylanase Using Brewer's Spent Grain as Substrate

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Adriana Knob ◽  
Susan Michelz Beitel ◽  
Diana Fortkamp ◽  
César Rafael Fanchini Terrasan ◽  
Alex Fernando de Almeida
Keyword(s):  
Xylanase Activity ◽  
Stationary Condition ◽  
Purification And Characterization ◽  
Xylanase Production ◽  
Brewer’S Spent Grain ◽  
Agroindustrial Waste ◽  
Sds Page ◽  
Exclusion Chromatography ◽  
Spent Grain

In recent decades, xylanases have been used in many processing industries. This study describes the xylanase production byPenicillium glabrumusing brewer's spent grain as substrate. Additionally, this is the first work that reports the purification and characterization of a xylanase using this agroindustrial waste. Optimal production was obtained whenP. glabrumwas grown in liquid medium in pH 5.5, at 25 °C, under stationary condition for six days. The xylanase fromP. glabrumwas purified to homogeneity by a rapid and inexpensive procedure, using ammonium sulfate fractionation and molecular exclusion chromatography. SDS-PAGE analysis revealed one band with estimated molecular mass of 18.36 kDa. The optimum activity was observed at 60 °C, in pH 3.0. The enzyme was very stable at 50 °C, and high pH stability was verified from pH 2.5 to 5.0. The ion Mn2+and the reducing agentsβ-mercaptoethanol and DTT enhanced xylanase activity, while the ions Hg2+, Zn2+, and Cu2+as well as the detergent SDS were strong inhibitors of the enzyme. The use of brewer's spent grain as substrate for xylanase production cannot only add value and decrease the amount of this waste but also reduce the xylanase production cost.

scholarly journals Optimization of production and partial characterization of xylanase from a newly isolated Bacillus amyloliquefaciens

2020 ◽  
Vol 42 ◽  
pp. e9
Author(s):  
Bruno Las-Casas Chaves ◽  
Ana Paula Martinazzo ◽  
Brisabella Coca ◽  
Adriane Nunes De Souza ◽  
Carlos Eduardo Teodoro
Keyword(s):  
Carbon Sources ◽  
Xylanase Activity ◽  
Residual Activity ◽  
Inoculum Size ◽  
Production Optimization ◽  
Partial Characterization ◽  
Birchwood Xylan ◽  
Xylanase Production ◽  
Local Soil

This paper reports the process of production optimization and partial characterization of xylanase from a newly isolated Bacillus amyloliquefacies VR002, isolated from local soil. The microorganism exhibited maximum xylanase production when 1.0% (v/v) of inoculum size was added to culture medium with initial pH 6, 1.0% (w/v) birchwood xylan, at 35 °C after 48h of incubation. Xylanase production in different carbon sources apart from birchwood xylan and xylose did not show high production levels. Optimum pH for xylanase activity was 6.0. The enzyme was alkali-stable and retained 100% of residual activity over the pH range from 6.0 to 10.0 for 24 h at 25°C. Optimum temperature for enzyme activity was 55°C. Xylanase was 100% stable at 4°C and 25°C even after 24h of incubation, a desirable characteristic for enzyme storage. Moreover, best crude extract volume and time reaction were found to be 10 µL and 5 min, respectively. After optimization of production and activity parameters, an increase of nearly 60-fold in xylanase activity (44.12 ± 4.36 U/mL) was achieved. Characteristics of B. amyloliquefaciens VR002 xylanase are particularly desirable for biotechnological applications

scholarly journals Purification and evaluation for effects of temperature on extracellular xylanase activity from Aspergillus oryzae DSM 1863

2017 ◽  
Vol 8 (1) ◽  
pp. 9-13
Author(s):  
Thi Tuyen Do ◽  
Sy Le Thanh Nguyen ◽  
Thi Thao Nguyen
Keyword(s):  
Aspergillus Oryzae ◽  
Specific Activity ◽  
Xylanase Activity ◽  
Residual Activity ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
Birch Wood ◽  
Sds Page ◽  
Birch Wood Xylan ◽  
Effects Of Temperature

Xylanase was purified from the crude culture of Aspergillus oryzae DSM1863 by sephadex G200 and DEAE – cellulose ion exchange chromatography. The molecular mass of the purified xylanase determined by SDS–PAGE was 21 kDa with a specific activity of 6768 U/mg towards 1% (w/v) of birch wood xylan. The optimum temperature was observed at 60°C. The enzyme was thermostable in the temperature range of 37-50°C with a high residual activity of 62-74% (650.6-775.9 U/mg protein). Enzyme xylanase được tinh sạch từ dịch lên men của chủng Aspergillus oryzae DSM1863 sau khi qua cột sắc ký lọc gel sephadex G200 và sắc ký trao đổi ion DEAE – cellulose. Khối lượng phân tử của enzyme xylanase tinh sạch được xác định bằng điên di đồ SDS- PAGE. Xylanase tinh sạch có kích thước là 21 kDa với hoạt tính đặc hiệu đạt 6768 U/mg sau khi được xác định với nồng độ cơ chất là 1% birch wood xylan. Nhiệt độ tối ưu để enzyme hoạt động mạnh nhất là 60C. Enzyme xylanase khá bền nhiệt. Hoạt tính của enzyme vẫn còn duy trì 62-74% (hoạt tính đặc hiệu đạt 650.6-775.9 U/mg protein) sau khi 8 giờ ủ ở 37-50°C.

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