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T Satyanarayana - One of the best experts on this subject based on the ideXlab platform.
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improved phytase production by a thermophilic mould Sporotrichum thermophile in submerged fermentation due to statistical optimization
Bioresource Technology, 2008Co-Authors: Ijende Singh, T SatyanarayanaAbstract:Abstract Culture variables affecting phytase production by a thermophilic mould Sporotrichum thermophile in submerged fermentation were optimized. Soluble starch, peptone, Tween-80 and sodium phytate were identified by Plackett–Burman design as the most significant factors to affect phytase production. The 24 full factorial central composite design of response surface methodology was applied for optimizing the concentrations of the significant variables and to delineate their interactions. Starch, Tween-80, peptone and sodium phytate at 0.4%, 1.0%, 0.3% and 0.3% supported maximum enzyme titres, respectively. An overall 3.73-fold improvement in phytase production was achieved due to optimization. When sodium phytate was substituted with wheat bran (3%), the phytase titre in the former was comparable with that in the latter.
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a marked enhancement in phytase production by a thermophilic mould Sporotrichum thermophile using statistical designs in a cost effective cane molasses medium
Journal of Applied Microbiology, 2006Co-Authors: Ijende Singh, T SatyanarayanaAbstract:Aims: Statistical optimization of phytase production by a thermophilic mould Sporotrichum thermophile in a cost-effective cane molasses medium. Methods and Results: Sporotrichum thermophile secreted phytase in cane molasses medium at 45°C and 250 rev min−1 after 5 days. The important factors identified by Plackett–Burman design (magnesium sulfate, Tween 80, ammonium sulfate and incubation period) were further optimized by response surface methodology (RSM). An overall 107% improvement in phytase production was achieved due to optimization. Supplementation of the medium with inorganic phosphate repressed the enzyme synthesis. When inorganic phosphate was reduced from the cane molasses medium by treatment with calcium chloride, the enzyme production increased. The phytase activity was not affected by the enzyme treatment with trypsin and pepsin. Conclusions: A twofold increase in phytase production was achieved due to optimization using statistical designs in a cost-effective cane molasses medium. Significance and Impact of the Study: Phytase production was doubled due to optimization. The enzyme, being resistant to trypsin and pepsin, thermostable and acid stable, can find application in animal feed industry for improving nutritional status of the feed and combating environmental phosphorus pollution.
Paul Christakopoulos - One of the best experts on this subject based on the ideXlab platform.
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Structural Characterisation by ESI-MS of Feruloylated Arabino-oligosaccharides Synthesised by Chemoenzymatic Esterification
MDPI AG, 2007Co-Authors: Paul Christakopoulos, Evangelos Topakas, Henk A Schols, Edwin J Bakx, Christina VafiadiAbstract:The chemoenzymatic synthesis of feruloylated arabino-oligosaccharides has been achieved, using a feruloyl esterase type C from Sporotrichum thermophile (StFaeC).The structure of the feruloylated products was confirmed by ESI-MSn
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kenaf xylan a source of biologically active acidic oligosaccharides
Carbohydrate Polymers, 2006Co-Authors: M K Nacos, Petros Katapodis, Paul Christakopoulos, Christos Pappas, Dimitra Daferera, Petros A Tarantilis, Moschos G PolissiouAbstract:Abstract Two xylose-rich hemicellulose fractions were obtained from kenaf wood ( Hibiscus cannabinus L.) through a series of sequential extractions which dissociated xylans from other cell wall components. These fractions were subsequently used as substrates for the production of biologically active aldouronic acids. Incubation of the xylans with a family 10 Thermoascus aurantiacus endoxylanase resulted in the isolation of an aldotetrauronic acid as the main acidic oligosaccharide in the hydrolysis products. Enzymic hydrolysis with a family 11 Sporotrichum thermophile endoxylanase instead resulted in the isolation of a aldopentauronic acid as the main acidic oligosaccharide. The identity and purity of both xylans and aldouronic acids were assessed with solid-state FT-IR, solid-state and solution 13 C NMR spectroscopy.
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Optimization of xylanase production by Sporotrichum thermophile using corn cobs and response surface methodology
Engineering in Life Sciences, 2006Co-Authors: Petros Katapodis, V. Christakopoulou, Paul ChristakopoulosAbstract:A 3 2 central composite experimental design was performed with the aim of optimizing the production of xylanase by Sporotrichum thermophile grown on corn cobs in submerged cultures. Various carbon and nitrogen sources were consecutively optimized, and corn cobs and ammonium phosphate concentrations were selected as substrates to test the effect of two variables, i.e., both substrate concentrations, on xylanase production. A second-order quadratic model and a response surface method showed that the optimum conditions for xylanase production were 2.7 % [w/v] corn cobs and 0.7 % [w/v] ammonium phosphate. These optimum conditions were transferred to 7 L bioreactors, where activities as high as 56 U/mL were obtained.
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Bioconversion of ferulic acid into vanillic acid by the thermophilic fungus Sporotrichum thermophile
Lwt - Food Science and Technology, 2003Co-Authors: Evangelos Topakas, Dimitris Kekos, E. Kalogeris, B.j. Macris, Paul ChristakopoulosAbstract:Sporotrichum thermophile is capable of promoting the formation of vanillic acid during ferulic acid degradation. Ferulic acid metabolism by S. thermophile apparently occurred via the propenoic chai ...
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Production of β-Fructofuranosidase from Sporotrichum thermophile and Its Application in the Synthesis of Fructooligosaccharides
Food Biotechnology, 2003Co-Authors: Petros Katapodis, Emmanuel Kalogeris, Dimitris Kekos, Basil J. Macris, Paul ChristakopoulosAbstract:Production of β-fructofuranosidase from the thermophilic fungus Sporotrichum thermophile was studied. The effect of nitrogen source, as well as the type and concentration of carbon source on enzyme production was examined. The results from flask experiments were used for the production of the enzyme in 7-l bioreactors. β-Fructofuranosidase from Sporotrichum thermophile showed both transfructosylating and hydrolytic activities. It was optimally active at 60°C, while the optimal pHs for hydrolysis and transfructosylation were 4.0 and 6.0, respectively. Synthesis of fructooligosaccharides was maximized at 20% (w/v) initial sucrose concentration. The major sugar produced by the transfructosylating activity of the enzyme was 6-kestose.
Ijende Singh - One of the best experts on this subject based on the ideXlab platform.
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improved phytase production by a thermophilic mould Sporotrichum thermophile in submerged fermentation due to statistical optimization
Bioresource Technology, 2008Co-Authors: Ijende Singh, T SatyanarayanaAbstract:Abstract Culture variables affecting phytase production by a thermophilic mould Sporotrichum thermophile in submerged fermentation were optimized. Soluble starch, peptone, Tween-80 and sodium phytate were identified by Plackett–Burman design as the most significant factors to affect phytase production. The 24 full factorial central composite design of response surface methodology was applied for optimizing the concentrations of the significant variables and to delineate their interactions. Starch, Tween-80, peptone and sodium phytate at 0.4%, 1.0%, 0.3% and 0.3% supported maximum enzyme titres, respectively. An overall 3.73-fold improvement in phytase production was achieved due to optimization. When sodium phytate was substituted with wheat bran (3%), the phytase titre in the former was comparable with that in the latter.
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a marked enhancement in phytase production by a thermophilic mould Sporotrichum thermophile using statistical designs in a cost effective cane molasses medium
Journal of Applied Microbiology, 2006Co-Authors: Ijende Singh, T SatyanarayanaAbstract:Aims: Statistical optimization of phytase production by a thermophilic mould Sporotrichum thermophile in a cost-effective cane molasses medium. Methods and Results: Sporotrichum thermophile secreted phytase in cane molasses medium at 45°C and 250 rev min−1 after 5 days. The important factors identified by Plackett–Burman design (magnesium sulfate, Tween 80, ammonium sulfate and incubation period) were further optimized by response surface methodology (RSM). An overall 107% improvement in phytase production was achieved due to optimization. Supplementation of the medium with inorganic phosphate repressed the enzyme synthesis. When inorganic phosphate was reduced from the cane molasses medium by treatment with calcium chloride, the enzyme production increased. The phytase activity was not affected by the enzyme treatment with trypsin and pepsin. Conclusions: A twofold increase in phytase production was achieved due to optimization using statistical designs in a cost-effective cane molasses medium. Significance and Impact of the Study: Phytase production was doubled due to optimization. The enzyme, being resistant to trypsin and pepsin, thermostable and acid stable, can find application in animal feed industry for improving nutritional status of the feed and combating environmental phosphorus pollution.
Sunil K. Khare - One of the best experts on this subject based on the ideXlab platform.
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Sporotrichum thermophile Xylanases and Their Biotechnological Applications
Fungi in Extreme Environments: Ecological Role and Biotechnological Significance, 2019Co-Authors: Ayesha Sadaf, Syeda Warisul Fatima, Sunil K. KhareAbstract:Thermophilic fungi are very useful resources for bio-industries and bioprocesses due to the inherent stability of their enzymes. These enzymes enable industrial biocatalysis at high temperatures, with low risk of contamination and high reaction rates. Sporotrichum thermophile is a well-known thermophilic ascomycete producing an array of interesting enzymes. Keeping in mind the industrial potential of S. thermophile, this chapter addresses the relevance of this thermophilic mould as well as the different types of enzymes produced by it with a special reference for its xylanase. The S. thermophile xylanase exhibits many interesting biochemical properties like broad pH and heat stability along with the ability to utilise a large number of xylan substrates. The genome analysis of S. thermophile revealed the presence of several carbohydrate hydrolases making it potentially useful in biomass utilisation. Recently the S. thermophile xylanase has also been shown to be remarkably stable and catalytically active in as high as 50% (v/v) concentration of most commonly used ionic liquids, the green solvents used for pretreating and solubilising the lignocellulosic biomass. This property has been successfully exploited for one-pot in situ IL pretreatment and saccharification of wheat straw. Further, the proteomic and transcriptomic analysis supported the upregulated lignocellulolytic enzymes like xylanases, cellulases, glucosidases and pectinases. Lately the genome editing of S. thermophile by CRISPR-Cas system has been attempted using targeted mutations for its cellulase enzyme system which has eventually led to enhanced production levels. Thus, the future research on S. thermophile will help in developing a robust and potential strain for cost-effective biofuel generation.
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Proteomic profiling of Sporotrichum thermophile under the effect of ionic liquids: manifestation of an oxidative stress response.
3 Biotech, 2019Co-Authors: Ayesha Sadaf, Rajeshwari Sinha, Sunil K. KhareAbstract:Sporotrichum thermophile, a known producer of industrial enzymes exhibited stability in the presence of ionic liquids (ILs).The study reports, for the first time, the stress response of S. thermophile upon exposure to ILs. In vitro assay showed increased anti-oxidative enzyme levels indicating ROS-mediated oxidative stress by ILs. The proteomic profile and identification of differential proteins confirmed the fungal adaptations by (i) increased expression of glycolytic enzymes and ATP synthases (ii) downregulation of TCA cycle and protein synthesis machinery components (iii) expression of HSP70 and catalase/peroxidase. These changes are indicative of metabolic regulation of many important pathways and how ILs can be used to manipulate protein behavior.
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Induction of xylanase in thermophilic fungi Scytalidium thermophilum and Sporotrichum thermophile
Brazilian Archives of Biology and Technology, 2012Co-Authors: Chetna Joshi, Sunil K. KhareAbstract:ABSTRACT Regulation of xylanase production in two thermophilic fungi Scytalidium thermophilum and Sporotrichum thermophile was investigated. The expression of xylanase was found to be inducible in both the cases. Various carbon sources were tested so as to identify the inducers. Soy flour and oat spelt xylan induced maximum level of xylanase in Scytalidium thermophilum and Sporotrichum thermophile respectively. Induction of xylanase in Scytalidium thermophilum led to simultaneous induction of cellulase. The zymography of enzyme preparations revealed that different carbon sources caused differential expression of multiple isoforms of xylanase in Scytalidium thermophilum, but same isoforms were expressed by Sporotrichum thermophile irrespective of the carbon source used. Key words: Induction, isoforms, Xylanase, biobleaching * Author for correspondence: skhare@rocketmail.com INTRODUCTION Xylan is the principle type of hemicellulose. It is a heterogeneous polysaccharide consisting of a homopolymeric backbone of 1,4-linked-β-D-xylopyranose units and short chain branches including O-acetyl, α-L-arabinofuranosyl, α-D-glucuronyl residues (Whistler and Richards 1970). Xylan originating from different plant sources show differences in xylan branching and composition (Badhan et al. 2004). Cooperative action of multiple xylanases is required for xylan hydrolysis. These xylanases, therefore, have overlapping yet different specificities (Dekker and Richards 1976). The main activities involved in xylan hydrolysis are 1,4-β-xylanase and β-xylosidase (Polizeli et al. 2005). Presence of multiple forms of xylanases is reported in several microorganisms. Thermophilic fungi viz. Melanocarpus albomyces, Talaromyces byssochlamydoides (Hayashida et al. 1988), Humicola insolens (syn. Scytalidium thermophilum ) (Dusterhoft et al. 1997) , Chaetomium thermophile (Ganju et al. 1989), Myceliophthora sp (Badhan et al. 2004) are specially known to produce multiple xylanases. Xylanases (in general all endoglycanases) act against large polysaccharides. Because of their size, polysaccharides cannot pass through the cell membrane to trigger the response for the synthesis of xylanases. However it is believed that low molecular-mass soluble catabolites are released from the action of low, constitutive amounts of hydrolases on xylan polymers. These catabolites enter the cell and signal to stimulate the synthesis of the respective enzymes (Sachslehner et al. 1998). Thus, the xylanases can be quite specifically induced. Xylanases have attracted considerable research interest because of their potential application in the
Petros Katapodis - One of the best experts on this subject based on the ideXlab platform.
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kenaf xylan a source of biologically active acidic oligosaccharides
Carbohydrate Polymers, 2006Co-Authors: M K Nacos, Petros Katapodis, Paul Christakopoulos, Christos Pappas, Dimitra Daferera, Petros A Tarantilis, Moschos G PolissiouAbstract:Abstract Two xylose-rich hemicellulose fractions were obtained from kenaf wood ( Hibiscus cannabinus L.) through a series of sequential extractions which dissociated xylans from other cell wall components. These fractions were subsequently used as substrates for the production of biologically active aldouronic acids. Incubation of the xylans with a family 10 Thermoascus aurantiacus endoxylanase resulted in the isolation of an aldotetrauronic acid as the main acidic oligosaccharide in the hydrolysis products. Enzymic hydrolysis with a family 11 Sporotrichum thermophile endoxylanase instead resulted in the isolation of a aldopentauronic acid as the main acidic oligosaccharide. The identity and purity of both xylans and aldouronic acids were assessed with solid-state FT-IR, solid-state and solution 13 C NMR spectroscopy.
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Optimization of xylanase production by Sporotrichum thermophile using corn cobs and response surface methodology
Engineering in Life Sciences, 2006Co-Authors: Petros Katapodis, V. Christakopoulou, Paul ChristakopoulosAbstract:A 3 2 central composite experimental design was performed with the aim of optimizing the production of xylanase by Sporotrichum thermophile grown on corn cobs in submerged cultures. Various carbon and nitrogen sources were consecutively optimized, and corn cobs and ammonium phosphate concentrations were selected as substrates to test the effect of two variables, i.e., both substrate concentrations, on xylanase production. A second-order quadratic model and a response surface method showed that the optimum conditions for xylanase production were 2.7 % [w/v] corn cobs and 0.7 % [w/v] ammonium phosphate. These optimum conditions were transferred to 7 L bioreactors, where activities as high as 56 U/mL were obtained.
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Production of β-Fructofuranosidase from Sporotrichum thermophile and Its Application in the Synthesis of Fructooligosaccharides
Food Biotechnology, 2003Co-Authors: Petros Katapodis, Emmanuel Kalogeris, Dimitris Kekos, Basil J. Macris, Paul ChristakopoulosAbstract:Production of β-fructofuranosidase from the thermophilic fungus Sporotrichum thermophile was studied. The effect of nitrogen source, as well as the type and concentration of carbon source on enzyme production was examined. The results from flask experiments were used for the production of the enzyme in 7-l bioreactors. β-Fructofuranosidase from Sporotrichum thermophile showed both transfructosylating and hydrolytic activities. It was optimally active at 60°C, while the optimal pHs for hydrolysis and transfructosylation were 4.0 and 6.0, respectively. Synthesis of fructooligosaccharides was maximized at 20% (w/v) initial sucrose concentration. The major sugar produced by the transfructosylating activity of the enzyme was 6-kestose.