Films from oat spelt arabinoxylan plasticized with glycerol and sorbitol

2009 ◽  
Vol 114 (1) ◽  
pp. 457-466 ◽  
Author(s):  
Kirsi S. Mikkonen ◽  
Susanna Heikkinen ◽  
Annemai Soovre ◽  
Marko Peura ◽  
Ritva Serimaa ◽  
...  
Keyword(s):  
Oat Spelt

scholarly journals Penentuan Konsentrasi Optimum Oat Spelts Xylan pada Produksi Xilanase pari Aspergillus niger dalam Media PDB (Potato Dextrose Broth)

2009 ◽  
Vol 12 (1) ◽  
pp. 7-13
Author(s):  
Nies Suci Mulyani ◽  
Mukhammad Asy’ari ◽  
Heru Prasetiyoningsih
Keyword(s):  
Aspergillus Niger ◽  
Potato Dextrose Broth ◽  
Oat Spelt

Enzim xilanase dapat menghidrolisis xilan menjadi xilosa yang dapat dimanfaatkan untuk pembuatan gula xilosa. Enzim xilanase dapat di isolasi dari Aspergillus niger dan peningkatan produksi xilanase membutuhkan suatu induser yaitu oat spelt xylan. Penelitian ini dilakukan dengan tujuan untuk menentukan konsentrasi optimum oat spelt xylan terhadap produksi xilanase dan karakterisasi xilanase hasil isolasi. Produksi xilanase pada media PDB (Potato Dextrose Broth) dengan penambahan variasi konsentrasi oat spelt xylan yaitu 0,0%; 0,8%; 1,0%; 1,2% dan 1,4% untuk mengetahui konsentrasi optimum oat spelt xylan. Selanjutnya produksi xilanase dengan konsentrasi optimum oat spelt xylan, xilanase dimurnikan dengan metode fraksinasi amonium sulfat bertingkat dan diálisis dan uji aktivitas menggunakan metode DNS dan uji kadar protein dengan menggunakan metode Lowry and karakterisasi enzim xilanase meliputi suhu, pH dan waktu inkubasi. Hasil penelitian yang telah diperoleh konsentrasi optimum oat splet xylan yaitu 1,2% dengan aktivitas enzim xilanase sebesar 469,490 Unit/mg protein. Enzim xilanase hasil isolasi diperoleh aktivitas tertinggi pada F5 sebesar 10280,840 Unit/mg protein dan bekerja optimum pada kondisi suhu 40oC, pH 4,5, waktu inkubasi 28 menit dan aktivitas spesifik pada kondisi optimum sebesar 11829,159 Unit/mg Protrein.Kata Kunci: Aspergillus niger, Xilanase, Oat Splet Xylan

Exploration of members ofAspergillussectionsNigri,Flavi, andTerreifor feruloyl esterase production

2006 ◽  
Vol 52 (9) ◽  
pp. 886-892 ◽  
Author(s):  
Ourdia Bouzid ◽  
Eric Record ◽  
Michèle Asther ◽  
Mireille Haon ◽  
David Navarro ◽  
...  
Keyword(s):  
Sugar Beet ◽  
Methyl Esters ◽  
Type A ◽  
Sugar Beet Pulp ◽  
Feruloyl Esterase ◽  
Type B ◽  
Original Activity ◽  
Beet Pulp ◽  
Feruloyl Esterases ◽  
Oat Spelt

The ability of members of Aspergillus sections Nigri, Flavi, and Terrei to produce feruloyl esterases was studied according to their substrate specificity against synthetic methyl esters of hydroxycinnamic acids. Type A feruloyl esterases (FAEA), induced during growth on cereal-derived products, show a preference for the phenolic moiety of substrates that contain methoxy substitutions, as found in methyl sinapinate, whereas type B feruloyl esterases (FAEB) show a preference for the phenolic moiety of substrates that contain hydroxyl substitutions, as occurs in methyl caffeate. All the strains of Aspergillus section Nigri (e.g., A. niger and A. foetidus) were able to produce feruloyl esterases with activity profiles similar to those reported for FAEA and FAEB of A. niger when grown on oat–spelt xylan and sugar beet pulp, respectively. The two genes encoding these proteins, faeA and faeB, were identified by Southern blot analysis. The strains of Aspergillus sections Flavi (e.g., A. flavus, A. flavo-furcatus, and A. tamarii) and Terrei (e.g., A. terreus) were able to produce type A and type B enzymes. faeA was revealed in genomic DNA of these strains, and FAEA was determined by immunodetection in cultures grown in oat–spelt xylan. In addition, type B enzymes, not related to faeB, were efficiently induced by oat–spelt xylan and exhibited very original activity profiles on sugar beet pulp. This work confirms that the members of the genus Aspergillus are good feruloyl esterase producers.Key words: Aspergillus, Nigri, Flavi, Terrei, feruloyl esterase.

Effect of oat spelt and beech xylan on the gelling properties of kappa-carrageenan hydrogels

2011 ◽  
Vol 85 (3) ◽  
pp. 529-540 ◽  
Author(s):  
Ramavatar Meena ◽  
R. Lehnen ◽  
U. Schmitt ◽  
B. Saake
Keyword(s):  
Gelling Properties ◽  
Kappa Carrageenan ◽  
Oat Spelt

Application of the affinity binding of xylanases to oat-spelt xylan in the purification of endoxylanase CM-2 from Streptomyces chattanoogensis CECT 3336

1998 ◽  
Vol 50 (2) ◽  
pp. 284-287 ◽  
Author(s):  
C. L. López-Fernández ◽  
J. Rodríguez ◽  
A. S. Ball ◽  
J. L. Copa-Patiño ◽  
M. I. Pérez-Leblic ◽  
...  
Keyword(s):  
Affinity Binding ◽  
Streptomyces Chattanoogensis ◽  
Oat Spelt

scholarly journals Using Lignosellulose Waste as a Xylanase Production Media of Mold Isolated from Rice Straw of Coastal-field

2018 ◽  
Vol 19 (2) ◽  
pp. 117
Author(s):  
Esti Utarti ◽  
S. Siswanto
Keyword(s):  
Quantitative Analysis ◽  
Rice Straw ◽  
Wheat Bran ◽  
Enzyme Activities ◽  
Activity Index ◽  
Xylanase Activity ◽  
Basic Salt ◽  
Xylanase Production ◽  
Aspergillus Foetidus ◽  
Oat Spelt

Hemicellulose is one of lignocellulose waste component, so that xylanase is one of importance enzyme of lignocellulose waste biodegradation. Molds as main decomposer lignosellulose waste has enzyme activities higher than yeast and bacteria. The aim of the research is to find mold that have xylanolitic activity using lignocellulose waste as media production. The research consist of isolations and screening mols from coastal-field of watu Ulo Jember, xylanase production using lignocellulose waste and idntification of mold which has the highes xylanase activity. A total of 66 molds isolated from rice straw in coastal-field of Watu Ulo Jember. There were screened for their xylanase activity. In semiquantitatively screen on Oat Spelt Xylan plate, the result showed that 62 have xilanolytic activities. Based on clearing zone production, isolates ESW A1 (3.2), ESW A5 (3.1), ESW C 16 (3.26), ESW D4 (3.0) and ESW D15 (3.21) have xilanase activity index higher than others. Furthermore, quantitative analysis using wheat bran, rice straw and baggase in basic salt Mandel’s modification media showed that xylanase activity of isolate ESW D4 was higher on rice straw 3% as substrate production with activity 2.66 U/mL. Isolate ESW D4 identified as Aspergillus foetidus so that called as Aspergillus foetidus ESW D4. Keywords: rice straw, coastal-field, Aspergillus foetidus ESW-D

scholarly journals Oviposition and Development of Tribolium Castaneum Herbst (Coleoptera: Tenebrionidae) on Different Types of Flour

Agronomy ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1593
Author(s):  
Alison R. Gerken ◽  
James F. Campbell
Keyword(s):  
Tribolium Castaneum ◽  
Adult Stage ◽  
Gluten Free ◽  
Insect Infestation ◽  
Substantial Variation ◽  
Management Tools ◽  
Different Types ◽  
Major Pest ◽  
Coleoptera Tenebrionidae ◽  
Oat Spelt

The commercial availability of low-gluten or gluten-free flours has been increasing due to consumer demands, which raises new challenges for the management of stored product insects since little is known about the susceptibility of these flours to infestation. Here we measured oviposition and development of Tribolium castaneum, the red flour beetle, a major pest of wheat and rice mills, on 18 different commercially available flours (almond, amaranth, barley, buckwheat, cassava, coconut, corn, garbanzo, millet, oat, potato, quinoa, rice, rye, sorghum, spelt, teff, and wheat) to assess the level of risk. The average number of eggs laid was highest for teff flour, with wheat, rice, buckwheat, sorghum, barley, rye, and spelt flour also having high oviposition. The lowest oviposition was for potato, quinoa, amaranth and cassava. Holding the eggs laid in these flours and evaluating the ability to develop to the adult stage demonstrated that the average number of adult progeny was highest for teff and wheat, followed by buckwheat, rye, oat, spelt, and millet. In an experiment where single eggs were placed directly in flour, the highest percentage development was in barley, buckwheat, sorghum, spelt, teff, and wheat. Time for 50% of single eggs to develop to adults was quickest for sorghum, spelt, teff, and wheat, while sorghum, buckwheat, corn, spelt, and barley had the quickest development of 90% of eggs to reach adults. There was substantial variation among the different flours which indicates variation in risk of insect infestation. As consumer interest in these flours continues to grow and these alternative flours become more prevalent in food facilities, understanding what diets insects successfully infest is critical to developing management tools.

A role of xylanase, α-L-arabinofuranosidase, and xylosidase in xylan degradation

2003 ◽  
Vol 49 (1) ◽  
pp. 58-64 ◽  
Author(s):  
A.K.M Shofiqur Rahman ◽  
Naoyasu Sugitani ◽  
Masahiro Hatsu ◽  
Kazuhiro Takamizawa
Keyword(s):  
Value Added ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Penicillium Sp ◽  
Enzyme Mixture ◽  
Initial Ph ◽  
Xylanase Enzyme ◽  
Xylanolytic Enzyme ◽  
Xylanolytic Enzymes ◽  
Oat Spelt

Renewable natural resources such as xylans are abundant in many agricultural wastes. Penicillium sp. AHT-1 is a strong producer of xylanolytic enzymes. The sequential activities of its xylanase, α-L-arabinofuranosidase, and β-xylosidase on model hemicellulose oat–spelt xylan was investigated. Optimum production of the enzymes was found in culture containing oat–spelt xylan at 30°C and initial pH 7.0 after 6 days. The enzymes were partially purified by ammonium sulphate fractionation and anion-exchange chromatography on DEAE-Toyopearl 650 S. The apparent molecular mass was 21 kDa, and the protein displayed an "endo" mode of action. The xylanase exhibited glycotransferase activity. It synthesized higher oligosaccharides from the initial substrates, and xylotriose was the shortest unit of substrate transglycosylated. Xylanolytic enzymes (enzyme mixture) produced by this Penicillium sp. interacted cooperatively and sequentially in the hydrolysis of oat–spelt xylan in the following order: α-L-arabinofuranosidase [Formula: see text] xylanase [Formula: see text] β-xylosidase. All three enzymes exhibited optimal activity under the same conditions (temperature, pH, cultivation), indicating that they alone are sufficient to completely depolymerize the test xylan. Results indicate that the xylanolytic enzyme mixture of Penicillium sp. AHT-1 could be useful for bioconversion of xylan-rich plant wastes to value-added products.Key words: xylanase, enzyme purification, enzymatic hydrolysis, Penicillium sp. AHT-1.

Extracellular Xylanase Production by Two Thermophilic Alkali-Tolerant Bacillus Strains in Batch and Continuous Cultures

2000 ◽  
Vol 55 (1-2) ◽  
pp. 66-69 ◽  
Author(s):  
Elka I. Emanuilova ◽  
Plamen L. Dimitrov ◽  
Rossica D. Mandeva ◽  
Margarita S. Kambourova ◽  
Stefan A. Engibarov
Keyword(s):  
Dilution Rate ◽  
Enzyme Synthesis ◽  
Bacillus Sp ◽  
Continuous Cultures ◽  
Xylanase Production ◽  
Batch Cultures ◽  
Bacillus Strains ◽  
Oat Spelt

Abstract Xylanase production of newly isolated thermophilic alkali-tolerant Bacillus sp. strain SP and strain BC was investigated in batch and continuous cultures. Enzyme synthesis was inducible with both strains and was observed only in xylan-containing media. Xylan from oat spelt is a better inducer than xylan from birch for strain Bacillus sp. BC while such difference was not observed for strain SP Compared with batch cultures xylanase production of both strains increased about two times and its rate became more than four times faster in continuous cultures at a dilution rate of 0.2 h-1.

Characteristics of a cluster of xylanase genes inFibrobacter succinogenesS85

2003 ◽  
Vol 49 (3) ◽  
pp. 171-180 ◽  
Author(s):  
Hyun S Jun ◽  
Jong K Ha ◽  
Laercio M Malburg, Jr. ◽  
Ann M Verrinder Gibbins ◽  
Cecil W Forsberg
Keyword(s):  
Catalytic Domain ◽  
Specific Activity ◽  
Glycosyl Hydrolase ◽  
Amino Acid Sequences ◽  
Pcr Analysis ◽  
Carbohydrate Binding ◽  
Fibrobacter Succinogenes ◽  
Rt Pcr ◽  
Ph Optimum ◽  
Oat Spelt

Xylanase genes xyn10D, xyn10E, and xyn10B, located sequentially on the Fibrobacter succinogenes S85 chromosome, were separately cloned and their properties characterized. Analysis of the sequences documented that xylanases Xyn10D, Xyn10E, and Xyn10B each consist of an N-terminal catalytic domain (glycosyl hydrolase family 10) and a C-terminal carbohydrate-binding module (CBM, family 6) connected by proline-rich linker sequences. The amino acid sequences exhibited similarities of between 53 and 60%. The xyn10D, xyn10E, and truncated xyn10BΔCBM were expressed in Escherichia coli and purified to homogeneity. The purified Xyn10D, Xyn10E, and Xyn10BΔCBM exhibited the same temperature optimum (40°C) and pH optimum (6.5) and the highest specific activity against arabinoxylan, oat spelt xylan, and birchwood xylan, respectively. Xyn10D exhibited an affinity for cellulose and xylan with 47 and 33% binding, respectively, while the truncated Xyn10DΔCBM did not bind to the substrates. The main hydrolysis products of the three xylanases acting on oat spelt xylan and arabinoxylan were xylose and xylobiose. RT-PCR analysis showed that the three genes were co-transcribed as a single transcript. Western immunoblot analysis revealed that the three xylanases were expressed at a very low level by F. succinogenes grown on either glucose or cellulose as the source of carbohydrate.Key words: Fibrobacter succinogenes S85, xylan, xylanase, clustered genes, RT-PCR.

Cloning of a xylanase gene from Fibrobacter succinogenes 135 and its expression in Escherichia coli

1991 ◽  
Vol 37 (7) ◽  
pp. 554-561 ◽  
Author(s):  
Y. J. Hu ◽  
D. C. Smith ◽  
K. -J. Cheng ◽  
C. W. Forsberg
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Xylanase Activity ◽  
Ecori Fragment ◽  
Fibrobacter Succinogenes ◽  
Host Bacterium ◽  
Xylanase Gene ◽  
E Coli ◽  
Cloned Gene ◽  
Oat Spelt

A genomic library consisting of 4- to 7-kb EcoRI DNA fragments from Fibrobacter succinogenes 135 was constructed using a phage vector, λgtWESλB, and Escherichia coli ED8654 as the host bacterium. Two positive plaques, designated λFSX101 and λFSX102, were identified. The inserts were 10.5 and 9.8 kb, respectively. A 2.3-kb EcoRI fragment that was subcloned from λFSX101 into pBR322 also showed xylanase activity. Southern blot analysis showed that the cloned EcoRI fragment containing the xylanase gene had originated from F. succinogenes 135. The cloned endo-(1,4)-β-D-xylanase gene (pFSX02) was expressed constitutively in E. coli HB101 when grown on LB and on M9 medium containing either glucose or glycerol as the carbon source. Most of the β-D-xylanase activity was located in the periplasmic space. Zymogram activity stains of nondenaturing polyacrylamide gels and isoelectric focusing gels showed that several xylanase isoenzymes were present in the periplasmic fraction of the E. coli clone FSX02 and they probably were due to posttranslational modification of a single gene product. Comparison of the FSX02 xylanase and the xylanase from the extracellular culture fluids of F. succinogenes 135 and S85 for their ability to degrade oat spelt xylan showed that, for equal units of β-D-xylanase activity, hydrolysis by the cloned gene product was more complete. However, unlike the unfractionated mixture of xylanases from F. succinogenes 135 and S85, the enzyme from E. coli FSX02 was unable to release arabinose from oat spelt xylan. Key words: rumen bacterium, xylanase gene, λgtWESλB, cellulolysis, Fibrobacter succinogenes.

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