Relevant bibliographies by topics / Xylanolytic and chitinolytic enzymes

Academic literature on the topic 'Xylanolytic and chitinolytic enzymes'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Xylanolytic and chitinolytic enzymes"

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Sousa, Carla da Silva, Ana Cristina Fermino Soares, and Marlon da Silva Garrido. "Characterization of streptomycetes with potential to promote plant growth and biocontrol." Scientia Agricola 65, no. 1 (February 2008): 50–55. http://dx.doi.org/10.1590/s0103-90162008000100007.

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Studies with streptomycetes in biocontrol programs and plant growth promotion are presented as technological alternatives for environmental sustainable production. This work has the objective of characterizing six isolates of streptomycetes aiming the production of extracellular enzymes, indole acetic acid, capacity for phosphate solubilization, root colonization and growth under different pH and salinity levels. For detection of enzyme activity the isolates were grown in culture media with the enzyme substrates as sole carbon source. The root colonization assay was performed on tomato seedlings grown on 0.6% water-agar medium. Growth under different pH and salinity levels was evaluated in AGS medium with 1%, 1.5%, 2%, 2.5%, and 3% NaCl, and pH levels adjusted to 5.0, 5.5, 6.0, 6.5, and 7.0. All isolates produced the enzymes amylase, catalase, and lipase, as well as indole acetic acid. With one exception (AC-92), all isolates presented cellulolytic and chitinolytic activity, and only AC-26 did not show xylanolytic activity. The isolates AC-147, AC-95, and AC-29 were the highest producers of siderophores. The isolates AC-26 and AC-29 did not show capacity for phosphate solubilization. All isolates colonized tomato roots in vitro, and AC-92 grew under all pH and salinity levels tested. The streptomycetes tested were considered as potential biocontrol and plant growth promotion agents.
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Patil, Reetarani S., Vandana Ghormade, and Mukund V. Deshpande. "Chitinolytic enzymes: an exploration." Enzyme and Microbial Technology 26, no. 7 (April 2000): 473–83. http://dx.doi.org/10.1016/s0141-0229(00)00134-4.

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KOGA, Daizo. "Chitinolytic enzymes in insects." Journal of the agricultural chemical society of Japan 62, no. 8 (1988): 1234–38. http://dx.doi.org/10.1271/nogeikagaku1924.62.1234.

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Kelly, C. T., M. R. O'Mahony, and W. M. Fogarty. "Extracellular xylanolytic enzymes ofPaecilomyces varioti." Biotechnology Letters 11, no. 12 (December 1989): 885–90. http://dx.doi.org/10.1007/bf01026846.

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Govinda Rajulu, Meenavalli B., Nagamani Thirunavukkarasu, Trichur S. Suryanarayanan, Jagadesan P. Ravishankar, Nour Eddine El Gueddari, and Bruno M. Moerschbacher. "Chitinolytic enzymes from endophytic fungi." Fungal Diversity 47, no. 1 (November 5, 2010): 43–53. http://dx.doi.org/10.1007/s13225-010-0071-z.

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Galanopoulou, Anastasia P., Irini Haimala, Daphne N. Georgiadou, Diomi Mamma, and Dimitris G. Hatzinikolaou. "Characterization of the Highly Efficient Acid-Stable Xylanase and β-Xylosidase System from the Fungus Byssochlamys spectabilis ATHUM 8891 (Paecilomyces variotii ATHUM 8891)." Journal of Fungi 7, no. 6 (May 29, 2021): 430. http://dx.doi.org/10.3390/jof7060430.

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Two novel xylanolytic enzymes, a xylanase and a β-xylosidase, were simultaneously isolated and characterized from the extracellular medium of Byssochlamys spectabilis ATHUM 8891 (anamorph Paecilomyces variotii ATHUM 8891), grown on Brewer’s Spent Grain as a sole carbon source. They represent the first pair of characterized xylanolytic enzymes of the genus Byssochlamys and the first extensively characterized xylanolytic enzymes of the family Thermoascaceae. In contrast to other xylanolytic enzymes isolated from the same family, both enzymes are characterized by exceptional thermostability and stability at low pH values, in addition to activity optima at temperatures around 65 °C and acidic pH values. Applying nano-LC-ESI-MS/MS analysis of the purified SDS-PAGE bands, we sequenced fragments of both proteins. Based on sequence-comparison methods, both proteins appeared conserved within the genus Byssochlamys. Xylanase was classified within Glycoside Hydrolase family 11 (GH 11), while β-xylosidase in Glycoside Hydrolase family 3 (GH 3). The two enzymes showed a synergistic action against xylan by rapidly transforming almost 40% of birchwood xylan to xylose. The biochemical profile of both enzymes renders them an efficient set of biocatalysts for the hydrolysis of xylan in demanding biorefinery applications.
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Li, Xinxin, Adiphol Dilokpimol, Mirjam A. Kabel, and Ronald P. de Vries. "Fungal xylanolytic enzymes: Diversity and applications." Bioresource Technology 344 (January 2022): 126290. http://dx.doi.org/10.1016/j.biortech.2021.126290.

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Sunna, A., and G. Antranikian. "Xylanolytic Enzymes from Fungi and Bacteria." Critical Reviews in Biotechnology 17, no. 1 (January 1997): 39–67. http://dx.doi.org/10.3109/07388559709146606.

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Gandhi, Jagruti P., and K. Koteshwara Rao. "Location of xylanolytic enzymes inChaetomium globosum." Journal of Basic Microbiology 37, no. 2 (1997): 79–84. http://dx.doi.org/10.1002/jobm.3620370202.

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Sekiguchi, Junichi, Masahiro Matsumiya, and Atsushi Mochizuki. "Distribution of Chitinolytic Enzymes in Seaweeds." Fisheries science 61, no. 5 (1995): 876–81. http://dx.doi.org/10.2331/fishsci.61.876.

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Dissertations / Theses on the topic "Xylanolytic and chitinolytic enzymes"

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McKenna, Ellen Margaret. "Xylanolytic enzymes of Ceraceomyces sublaevis." Thesis, University of Ulster, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.333973.

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O'Donnell, Raymond William. "Chitinolytic enzymes of Candida albicans." Thesis, University of Aberdeen, 1991. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=158392.

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It has been envisaged that lytic enzymes may be crucial in determining the morphology and growth of fungi, and may therefore represent a target for antifungal agents. The chitinolytic system of Candida albicans was investigated using a range of 4-methylumbelliferyl glycosides as model substrates, and its potential as a target for antibiotics has been assessed. Maximum hydrolysis was obtained with substrates having monomer and tetramer chain lengths, being attributed to N-acetylglucosaminidase and endochitinase respectively. Activities were investigated in cell fractions, vacuoles, and also in whole cell preparations. The characteristics of both chitinase and N-acetylglucosaminidase were examined, including pH and temperature optima and Km values. Chitinase was semi-purified on Fast Protein Liquid chromatography system and activity could be located after native polyacrylamide gel electrophoresis. Analysis of chitinase activity during the growth of the yeast morphology of C.albicans revealed maximal activities during the logarithmic phase, suggesting a relationship of chitinase levels to active growth of the pathogen. It was found that the antibiotic allosamidin was a potent inhibitor of chitinase activity of C.albicans, but not of N-acetylglucosaminidase. Conversely, an analogue of N-acetylglucosamine was found to be a potent inhibitor of N-acetylglucosaminidase but not of chitinase. Treatment of yeast suspensions with allosamidin resulted in an increased chain length. No cell death, or discernible pattern of change in the radiolabelling was observed in the presence of either allosamidin or N-acetylglucosamine analogue. Similarly no consistent change in the optical density of cultures was observed in the presence of either inhibitor. Even in the presence of the membrane permeabilising agent amphotericin no effects were observed above those achieved with amphotericin alone. Comparative studies were carried out upon the chitinolytic activity of Kluyveromyces lactis toxin and bovine serum. The chitin synthetic system of Benjaminiella poitrasii was compared to that of C.albicans.
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Manson, Forbes Donald Castell. "Chitinolytic enzymes of turbot, Scophthalmus maximus (L.)." Thesis, University of Aberdeen, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.277191.

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Kellett, Louise Elizabeth. "The molecular biology of xylanolytic enzymes from Pseudomonas fluorescens subsp. cellulosa." Thesis, University of Newcastle Upon Tyne, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315636.

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Oree, Glynis. "Chitin hydrolysis with chitinolytic enzymes for the production of chitooligomers with antimicrobial properties." Thesis, Rhodes University, 2019. http://hdl.handle.net/10962/67887.

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There are many diseases and illnesses in the world that require new drug treatments and chitin has been shown to produce chitooligomeric derivatives which exhibit promising antimicrobial and immune-enhancing properties. However, the rate-limiting step is associated with the high recalcitrance of chitinous substrates, and low hydrolytic activities of chitinolytic enzymes, resulting in low product release. To improve and create a more sustainable and economical process, enhancing chitin hydrolysis through various treatment procedures is essential for obtaining high enzyme hydrolysis rates, resulting in a higher yield of chitooligomers (CHOS). In literature, pre-treatment of insoluble biomass is generally associated with an increase in accessibility of the carbohydrate to hydrolytic enzymes, thus generating more products. The first part of this study investigated the effect of alkali- (NaOH) and acid pre-treatments (HCl and phosphoric acid) on chitin biomass, and chemical and morphological modifications were assessed by the employment of scanning electron microscopy (SEM), Fourier Transform Infrared Spectroscopy (FTIR), Energy-Dispersive X-ray spectrometery (EDX) and x-ray diffraction (XRD). Data obtained confirmed that pre-treated substrates were more chemically and morphologically modified. These results confirmed the fact that pre-treatment of chitin disrupts the structure of the biomass, rendering the polymer more accessible for enzymatic hydrolysis. The commercial chitinases from Bacillus cereus and Streptomyces griseus (CHB and CHS) are costly. Bio-prospecting for other chitin-degrading enzymes from alternate sources such as Oidiodendron maius, or the recombinant expression of CHOS, was a more economically feasible avenue. The chit1 gene from Thermomyces lanuginosus, expressed in Pichia pastoris, produced a large range CHOS with a degree of polymerisation (DP) ranging from 1 to above 6. TLC analysis showed that O. maius exhibited chitin-degrading properties by producing CHOS with a DP length of 1 to 3. These two sources were therefore successful in producing chitin-degrading enzymes. The physico-chemical properties of commercial (CHB and CHS) and expressed (Chit1) chitinolytic enzymes were investigated, to determine under which biochemical conditions and on which type of biomass they can function on optimally, for the production of value-added products such as CHOS. Substrate affinity assays were conducted on the un-treated and pre-treated biomass. TLC revealed that chitosan hydrolysis by the commercial chitinases produced the largest range of CHOS with a DP length ranging from 1 to 6. A range of temperatures (35-90oC) were investigated and CHB, CHS and Chit1 displayed optimum activities at 50, 40 and 45 oC, respectively. Thermostability studies that were conducted at 37 and 50oC revealed that CHB and CHS were most stable at 37oC. Chit1 showed great thermostablity at both temperatures, rendering this enzyme suitable for industrial processes at high temperatures. pH optima studies demonstrated that the pH optima for CHB, CHS and Chit1 was at a pH of 5.0, with specific activities of 33.459, 46.2 and 5.776 μmol/h/mg, respectively. The chain cleaving patterns of the commercial enzymes were determined and exo-chitinase activity was exhibited, due to the production of CHOS that were predominantly of a DP length of 2. Enzyme binary synergy studies were conducted with commercial chitinases (CHB and CHS) on colloidal chitin. Studies illustrated that the simultaneous combination of CHB 75%: CHS 25% produced the highest specific activity (3.526 μmol/h/mg), with no synergy. TLC analysis of this enzyme combination over time revealed that predominantly chitobiose was produced. This suggested that the substrate crystallinity and morphology played an important role in the way the enzymes cleaved the carbohydrate. Since CHOS have shown great promise for their antimicrobial properties, the CHOS generated from the chitinous substrates were tested for antimicrobial properties on Bacillus subtilis, Escherichia coli, Klebsiella and Staphlococcus aureus. This study revealed that certain CHOS produced have inhibitory effects on certain bacteria and could potentially be used in the pharamceutical or medical industries. In conclusion, this study revealed that chitinases can be produced and found in alternate sources and be used for the hydrolysis of chitinous biomass in a more sustainabe and economically viable manner. The chitinases investigated (CHB, CHS and Chit1) exhibited different cleaving patterns of the chitinous substrates due to the chemical and morphological properties of the biomass. CHOS produced from chitinous biomass exhibited some inhibitory effects on bacterial growth and show potential for use in the medical industry.
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au, s. averis@murdoch edu, and Susana M. E. Severgnini. "Isolation and characterisation of two chitinase and one novel glucanase genes for engineering plant defence against fungal pathogens." Murdoch University, 2006. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20071213.105659.

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Hydrolytic enzymes such as chitinases and glucanases are implicated in plant defense responses against fungal pathogens. These enzymes are responsible for the breakdown of chitin and glucan, two major components of the fungal cell walls. Genes encoding these enzymes have been used to genetically engineer plants to enhance their protection against fungal pathogens. Western Australia has over 4000 endemic plant species and a largely unknown fungal biota. Given that fungi possessing chitinases and glucanases with novel activities have been isolated in other parts of the world, we propose that fungi from Western Australian soils may possess novel biochemical/enzymatic activities. The aims of this research project were to isolate chitinolytic and glucanolytic fungi from soil and to clone the genes encoding for chitinase and glucanase enzymes. To achieve these aims, fungi with activity against chitin and glucan were isolated, the activity quantified by colorimetric and inhibition assays and gene fragments with homology to known chitinase and glucanase genes were isolated and their sequences determined. Soil fungi were isolated from five locations in and around the Perth Metropolitan area of Western Australia with the use of a medium containing Rose Bengal that eliminates all actinomycetes and most bacteria and reduces the growth of fast growing mold colonies. Forty-one isolates were obtained by this method. Twenty four chitinolytic and glucanolytic fungal isolates were identified by growing them on chitin-containing media to select for those species that utilised chitin/glucan as a carbon source. These were assayed for production of exo- and endochitinolytic and glucanolytic enzymes. Enzyme activity was compared between crude and dialysed supernatants. Exochitinase activity was determined in the supernatants of 4-day old fungal cultures by the release of p-nitrophenol from p-nitrophenyl-N-acetyl-â-D glucosaminide. The supernatants were measured for endochitinase activity determined by the reduction of turbidity of suspensions of colloidal chitin. Glucanase activity was determined by release of reducing sugar (glucose) from laminarin. Supernatants from eleven of the twenty four isolates showed significant levels of enzyme activity. Eleven isolates were assayed for activity against purified cell walls of phytopathogenic fungi. Activity was determined by measuring reducing sugars in the fungal supernatants against cell wall preparations of six economically important plant pathogens. Chitinolytic activity was detected in seven isolates against cell wall preparations of Botrytis cinerea and Rhizoctonia solani, in four isolates against Fusarium solani and Sclerotinia sclerotium; in five isolates against Ascochyta faba and in six isolates against Leptosphaeria maculans. Similarly glucanolytic activity was detected in eight isolates against B. cinerea, in seven against R. solani, in two against F. solani, in three against S. sclerotium and A. faba and in one against L. maculans. The supernatants derived from the isolates were used in a bioassay to determine growth inhibition against live B. cinerea spores by measuring turbidity reduction. Growth inhibition was measured against a control (B. cinerea, grown in medium with no added supernatant). Boiled supernatant did not inhibit the growth of B. cinerea spores but there was 100% inhibition by the crude supernatant from ten of the twenty four isolates. Similarly, supernatants were used to assess growth inhibition against live mycelia cultures of F. solani and S. sclerotium. Growth inhibition of F solani ranged from 9- 59%, boiled and crude supernatants respectively whilst growth inhibition of S. sclerotium ranged from 46-75%, boiled and crude supernatants respectively. Two partial chitinase genes from the soil filamentous ungus Trichoderma asperellum,(ChiA and ChiB) and a novel glucanase gene from the filamentous fungus Aspergillus (Glu1) were cloned. ChiA, was 639 bp long, encoding 191 amino acids with identity to other chitinase genes. Two highly conserved regions, characteristic of glycosyl hydrolases from family 18, were present. ChiB, was 887 bp long and encoded a 293 amino acid sequence that was closely related to an endochitinase gene from the filamentous fungus Trichoderma asperellum. The two highly conserved regions corresponding to the substrate binding and active sites that characterise the glycosyl hydrolases from family 18, also found in ChiA, were found in this gene. Glu1 was 2844 bp long and encoded a 948 amino acid sequence that shared high identity with a â-1, 3-glucanase from the filamentous fungus Aspergillus oryzae. The sequence contained conserved regions found in glycosyl hydrolases from family 17 that encode for substrate binding, N-terminal sequences and putative asparagine linked glycosylation sites. The partial putative sequence ChiA is probably a pseudogene because it has two inframe stop codons. However, once the entire sequence of ChiB is known, both ChiB and the novel glucanase gene Glu1 could be useful contenders for engineering resistance in crop plants.
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LeCleir, Gary R. "Chitinolytic bacteria and enzymes from Mono Lake, CA, USA." 2005. http://purl.galileo.usg.edu/uga%5Fetd/lecleir%5Fgary%5Fr%5F200512%5Fphd.

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Thesis (Ph. D.)--University of Georgia, 2005.
Directed by James T. Hollibaugh. Includes an article published in Applied and environmental microbiology, and articles submitted to Aquatic microbial ecology, and Applied and environmental microbiology. Includes bibliographical references.
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Chen, Chun-Jen, and 陳俊任. "Studies on Chitinolytic Enzymes from Aeromonas sp. No. 16." Thesis, 1993. http://ndltd.ncl.edu.tw/handle/24841666705890767379.

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碩士
國立臺灣大學
農業化學系
81
The partially hydrolyzed products of chitin and chitosan, N- acetylchitooligosaccharides and chitooligosaccharides, are of special interest because these oligosaccharides have been evalu- ated in various applications.This study focused on the production of N-acetylchitooligosaccharides by microbial enzymes. Crab shell chitin prepared by treating crab shell with acid and alkali was used as a substrate for isolating chitinolytic mi- croorganisms. Among the 103 isolated strains, strain No. 16 appeared to be the most potential chitinase-producing strain. It was identified belonging to the genus Aeromonas and named Aero- monas sp. No. 16. When the medium contained 1.5% colloidal chitin , 2.0% tryp- tone and 1.5% yeast extract with initial pH 10, Aeromonas sp. No. 16 could produce 1.4 units/milliliter of chitinase activity after 24 hours cultivation in 500 mL Hinton''''s flask. Using crys- talline chitin as substrate for enzyme productionin a 5L fermen- tor with temperature at 30℃, aeration at 1 vvm, agitation at 400 rpm and pH controlled between 7 and 8, chitinase activity could reach 1.5 units/milliliter after 30 hours cultivation. Chitin and N-acetylglucosamine were both found to be inducers for chitinase synthesis by Aeromonas sp. No. 16, on the other hand, addition of other carbohydrates would repress enzyme production with different degrees. Crude enzyme hydrolyzed chitin and produced N-acetylglucosa- mine as main product ,hydrolyzed chitosan with unknown products formation, which was supposed to be hetero- chitooligosaccharide. In crude enzyme, chitinase activity was most active at pH 6.0 and 50℃, and was stable at pH between 5 and 9 and at temperature be- low 40℃. β-N-acetyl-D- glucosaminidase was less stable at 40℃ and supposed to be an intracellular enzyme. After PAGE and acti-
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Lin, Yuan-Ju, and 林芫如. "Study on Chitinolytic Enzymes from Serratia marcescens NTU-17." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/44846555575249611399.

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碩士
國立臺灣大學
生物產業機電工程學研究所
96
Abstract N-acetylchitooligosaccharides (degree of polymerization 4-6) have specific biological activities such as antitumor activity and immuno-enhancing effects. In this study, we aimed to isolate environmental microorganisms which could produce enzymes to hydrolyze chitin into N-acetylchitooligosaccharides. At the initial stage, we hydrolyzed colloidal chitin with crude microbial enzymes and analyzed the products by HPLC. From this screening, we found that the crude enzyme from one bacterial isolate could hydrolyze chitin and produce N-acetylchitooligosaccharides. The bacterial strain was identified by 16S rRNA sequencing and phylogenetic analysis to belong Serratia marcescens and was named S. marcescens NTU-17. We used central composite design (CCD) of response surface methodology (RSM) to obtain the optimal culture condition for chitinase production: 0.4 g/l colloidal chitin, 1.6 g/l casein, 30。C and pH 7.5; the highest chitinase activity was produced at 18 hours after inoculation. The crude enzyme from culture broth of S. marcescens NTU-17 was subjected to successive steps of purification. After ammonium sulfate fractionation (35-70%), gel filtration-Sephacryl 200 chromatography, and DEAE-Sephacel column chromatography, two species of chitinase were purified and the molecular weights were determined by SDS-PAGE to be 53 kDa (chitinase 1) and 39 kDa (chitinase 2). The chitinase activity of chitinase 1 and 2 were also verified by an in-gel chitinase activity assay. After purification, the specific activity of chitinase was increased by 2.5 fold and the yield was 12%. Chitinase 1 exhibited the optimal activity at pH 3 and 50℃, and chitinase 2 showed the optimal activity at 30℃ and similar activities at pH 3-12.
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Wu, Li-Sen, and 吳立森. "Studies on chitinolytic enzymes from Aeromonas caviae No. 2." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/10837667822021624179.

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碩士
臺灣大學
微生物與生化學研究所
98
It was reported that N-acetylchitooligosaccharides (degree of polymerization 4-7) (GlcNAc)4-7 have specific biological activities such as antitumor activity and immuno-stimulating effects. In this study, we aimed to screen microorganisms from a chitin-rich environment and isolate the ones that can produce enzymes to hydrolyze chitin into N-acetylchitooligosaccharides. At the initial stage, we used the selection medium with colloidal chitin as the sole carbon source to select for microorganisms which could utilize chitin for growth. The microbial isolates were further screened by incubating the culture broth with colloidal chitin and analyzing the products by HPLC and TLC. Using this screening strategy, we obtained one bacterial isolate that could produce enzymes to hydrolyze chitin into (GlcNAc) 4-5 and hydrolyze chitosan into (GlcN/GlcNAc) 4-6. The bacterial strain was identified by 16S rDNA sequencing and phylogenetic classification to belong to Aeromonas caviae and was named Aeromonas caviae No. 2. To optimize the culture condition for producing higher amounts of chitinase, we first tested various culture pHs and temperatures and found that the highest chitinase activity was produced at pH 6 and 25℃. Using the central composite design (CCD) of response surface methodology (RSM), we further obtained the optimal concentrations of chitin and nitrogen sources in the culture medium to be colloidal chitin: 1.098%, soybean flour: 0.735% and yeast extract: 0.74%. The crude enzyme produced in selection medium went through successive steps of purification including ammonium sulfate precipitation (40-70%), chitin affinity-hydrolysis method and gel filtration chromatography (Sephacryl 200). After purification, four major proteins were found range from 55 to 100 kDa on the SDS-PAGE, and two of them showed chitinase activity range from 55 to 70 kDa on the in-gel chitinase activity assay. When proteins from the optimized culture medium were purified using nine major bands appeared range from 40 to 100 kDa on the SDS-PAGE, and three of them showed chitinase activity on the in-gel chitinase activity assay. Moreover, the purified proteins could hydrolyze chitin primarily into (GlcNAc)2 and hydrolyze chitosan into (GlcN/GlcNAc) 4-6.
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Books on the topic "Xylanolytic and chitinolytic enzymes"

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McKenna, Ellen Margaret. Xylanolytic enzymes of Ceraceomyces sublaevis. [S.l: The Author], 1993.

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Xylanolytic Enzymes. Elsevier Science & Technology Books, 2014.

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Xylanolytic Enzymes. Elsevier, 2014. http://dx.doi.org/10.1016/c2013-0-18577-7.

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Bajpai, Pratima. Xylanolytic Enzymes. Elsevier Science & Technology Books, 2014.

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Bajpai, Pratima. Microbial Xylanolytic Enzymes. Elsevier Science & Technology Books, 2023.

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Bajpai, Pratima. Microbial Xylanolytic Enzymes. Elsevier Science & Technology, 2022.

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Microbial Xylanolytic Enzymes. Elsevier, 2022. http://dx.doi.org/10.1016/c2021-0-02185-4.

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Book chapters on the topic "Xylanolytic and chitinolytic enzymes"

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Archana, A., A. Sharma, and T. Satyanarayana. "Xylanolytic Enzymes." In Thermophilic Moulds in Biotechnology, 169–90. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-015-9206-2_7.

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Tupe, Santosh G., Ejaj K. Pathan, Suman Ganger, Shweta Patil, and Mukund V. Deshpande. "Fungal Chitinolytic Enzymes." In Progress in Mycology, 185–201. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-3307-2_7.

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Zikakis, John P. "Chitinolytic Enzymes and Their Applications." In ACS Symposium Series, 116–26. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/bk-1989-0389.ch008.

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Poutanen, K., H. Härkönen, T. Parkkonen, K. Autio, T. Suortti, A. Kantelinen, and L. Viikari. "The Use of Xylanolytic Enzymes in Processing of Cereals." In Developments in Food Engineering, 72–74. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2674-2_16.

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Kintsu, Hiroyuki, Taiga Okumura, Lumi Negishi, Shinsuke Ifuku, Toshihiro Kogure, Shohei Sakuda, and Michio Suzuki. "Chitin Degraded by Chitinolytic Enzymes Induces Crystal Defects of Calcites." In Biomineralization, 375–81. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1002-7_40.

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Halder, Suman Kumar, Shilpee Pal, and Keshab Chandra Mondal. "Biosynthesis of Fungal Chitinolytic Enzymes and Their Potent Biotechnological Appliances." In Recent Advancement in White Biotechnology Through Fungi, 281–98. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-10480-1_8.

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Fawzya, Yusro Nuri, and Ekowati Chasanah. "Isolation of Chitinolytic Enzymes and Development of Chitooligosaccharides in Indonesia." In Chitooligosaccharides, 277–300. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-92806-3_17.

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Krogh, Kristian B. R., Astrid Mørkeberg, Henning Jørgensen, Jens C. Frisvad, and Lisbeth Olsson. "Screening Genus Penicillium for Producers of Cellulolytic and Xylanolytic Enzymes." In Proceedings of the Twenty-Fifth Symposium on Biotechnology for Fuels and Chemicals Held May 4–7, 2003, in Breckenridge, CO, 389–401. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1007/978-1-59259-837-3_34.

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Verma, Digvijay, Ravi Kumar, and Tulasi Satyanarayana. "Diversity in Xylan-degrading Prokaryotes and Xylanolytic Enzymes and Their Bioprospects." In Microbial Diversity in Ecosystem Sustainability and Biotechnological Applications, 325–73. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-8487-5_14.

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Cheba, Ben Amar. "Bacillus sp. R2: Promising Marine Bacterium with Chitinolytic/Agarovorant Activity and Multiple Enzymes Productivity." In The 15th International Conference Interdisciplinarity in Engineering, 13–24. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-93817-8_2.

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Conference papers on the topic "Xylanolytic and chitinolytic enzymes"

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Hassan, Shady S., Gwilym A. Williams, and Amit K. Jaiswa. "Fungus-Mediated Synthesis of magnetic nanoparticles for immobilisation of Pectolytic and xylanolytic enzymes." In The 6th World Congress on New Technologies. Avestia Publishing, 2020. http://dx.doi.org/10.11159/icnfa20.134.

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Reports on the topic "Xylanolytic and chitinolytic enzymes"

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Kloepper, Joseph W., and Ilan Chet. Endophytic Bacteria of Cotton and Sweet Corn for Providing Growth Promotion and Biological Disease Control. United States Department of Agriculture, January 1996. http://dx.doi.org/10.32747/1996.7613039.bard.

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Endophytes were isolated from 16.7% of surface-disinfested seeds and 100% of stems and roots of field-growth plants. Strains from Israel with broad-spectrum in vitro antibiosis were mainly Bacillus spp., and some were chitinolytic. Following dipping of cut cotton roots into suspensions of these strains, endophytes were detected up to 72 days later by isolation and by autoradiograms of 14C-labelled bacteria. Selected endophytes exhibited biological control potential based on significant reductions in disease severity on cotton inoculated with Rhizoctonia solani or Fusarium oxysporum f. sp. vasinfectum as well as control of Sclerotium rolfsii on bean. Neither salicylic acid nor chitinase levels increased in plants as a result of endophytic colonization, suggesting that the observed biocontrol was not accounted for by PR protein production. Some biocontrol endophytes secreted chitinolytic enzymes. Model endophytic strains inoculated into cotton stems via stem injection showed only limited movement within the stem. When introduced into stems at low concentrations, endophytes increased in population density at the injection site. After examining several experimental and semi-practical inoculation systems, seed treatment was selected as an efficient way to reintroduce most endophytes into plants.
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Harman, Gary E., and Ilan Chet. Enhancement of plant disease resistance and productivity through use of root symbiotic fungi. United States Department of Agriculture, July 2008. http://dx.doi.org/10.32747/2008.7695588.bard.

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The objectives of the project were to (a) compare effects ofT22 and T-203 on growth promotion and induced resistance of maize inbred line Mol7; (b) follow induced resistance of pathogenesis-related proteins through changes in gene expression with a root and foliar pathogen in the presence or absence of T22 or T-203 and (c) to follow changes in the proteome of Mol? over time in roots and leaves in the presence or absence of T22 or T-203. The research built changes in our concepts regarding the effects of Trichoderma on plants; we hypothesized that there would be major changes in the physiology of plants and these would be reflected in changes in the plant proteome as a consequence of root infection by Trichoderma spp. Further, Trichoderma spp. differ in their effects on plants and these changes are largely a consequence of the production of different elicitors of elicitor mixtures that are produced in the zone of communication that is established by root infection by Trichoderma spp. In this work, we demonstrated that both T22 and T-203 increase growth and induce resistance to pathogens in maize. In Israel, it was shown that a hydrophobin is critical for root colonization by Trichoderma strains, and that peptaibols and an expansin-like protein from Ttrichoderma probably act as elicitors of induced resistance in plants. Further, this fungus induces the jasmonate/ethylene pathway of disease resistance and a specific cucumber MAPK is required for transduction of the resistance signal. This is the first such gene known to be induced by fungal systems. In the USA, extensive proteomic analyses of maize demonstrated a number of proteins are differentially regulated by T. harzianum strain T22. The pattern of up-regulation strongly supports the contention that this fungus induces increases in plant disease resistance, respiratory rates and photosynthesis. These are all very consistent with the observations of effects of the fungus on plants in the greenhouse and field. In addition, the chitinolytic complex of maize was examined. The numbers of maize genes encoding these enzymes was increased about 3-fold and their locations on maize chromosomes determined by sequence identification in specific BAC libraries on the web. One of the chitinolytic enzymes was determined to be a heterodimer between a specific exochitinase and different endochitinases dependent upon tissue differences (shoot or root) and the presence or absence of T. harzianum. These heterodimers, which were discovered in this work, are very strongly antifungal, especially the one from shoots in the presence of the biocontrol fungus. Finally, RNA was isolated from plants at Cornell and sent to Israel for transcriptome assessment using Affymetrix chips (the chips became available for maize at the end of the project). The data was sent back to Cornell for bioinformatic analyses and found, in large sense, to be consistent with the proteomic data. The final assessment of this data is just now possible since the full annotation of the sequences in the maize Affy chips is just now available. This work is already being used to discover more effective strains of Trichoderma. It also is expected to elucidate how we may be able to manipulate and breed plants for greater disease resistance, enhanced growth and yield and similar goals. This will be possible since the changes in gene and protein expression that lead to better plant performance can be elucidated by following changes induced by Trichoderma strains. The work was in, some parts, collaborative but in others, most specifically transcriptome analyses, fully synergistic.
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