Academic literature on the topic 'Xylanolytic and chitinolytic enzymes'
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Journal articles on the topic "Xylanolytic and chitinolytic enzymes"
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.
Full textPatil, 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.
Full textKOGA, 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.
Full textKelly, 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.
Full textGovinda 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.
Full textGalanopoulou, 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.
Full textLi, 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.
Full textSunna, 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.
Full textGandhi, 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.
Full textSekiguchi, 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.
Full textDissertations / Theses on the topic "Xylanolytic and chitinolytic enzymes"
McKenna, Ellen Margaret. "Xylanolytic enzymes of Ceraceomyces sublaevis." Thesis, University of Ulster, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.333973.
Full textO'Donnell, Raymond William. "Chitinolytic enzymes of Candida albicans." Thesis, University of Aberdeen, 1991. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=158392.
Full textManson, 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.
Full textKellett, 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.
Full textOree, Glynis. "Chitin hydrolysis with chitinolytic enzymes for the production of chitooligomers with antimicrobial properties." Thesis, Rhodes University, 2019. http://hdl.handle.net/10962/67887.
Full textau, 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.
Full textLeCleir, Gary R. "Chitinolytic bacteria and enzymes from Mono Lake, CA, USA." 2005. http://purl.galileo.usg.edu/uga%5Fetd/lecleir%5Fgary%5Fr%5F200512%5Fphd.
Full textDirected 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.
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.
Full text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-
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.
Full text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.
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.
Full text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.
Books on the topic "Xylanolytic and chitinolytic enzymes"
McKenna, Ellen Margaret. Xylanolytic enzymes of Ceraceomyces sublaevis. [S.l: The Author], 1993.
Find full textXylanolytic Enzymes. Elsevier Science & Technology Books, 2014.
Find full textXylanolytic Enzymes. Elsevier, 2014. http://dx.doi.org/10.1016/c2013-0-18577-7.
Full textBajpai, Pratima. Xylanolytic Enzymes. Elsevier Science & Technology Books, 2014.
Find full textBajpai, Pratima. Microbial Xylanolytic Enzymes. Elsevier Science & Technology Books, 2023.
Find full textBajpai, Pratima. Microbial Xylanolytic Enzymes. Elsevier Science & Technology, 2022.
Find full textMicrobial Xylanolytic Enzymes. Elsevier, 2022. http://dx.doi.org/10.1016/c2021-0-02185-4.
Full textBook chapters on the topic "Xylanolytic and chitinolytic enzymes"
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.
Full textTupe, 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.
Full textZikakis, 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.
Full textPoutanen, 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.
Full textKintsu, 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.
Full textHalder, 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.
Full textFawzya, 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.
Full textKrogh, 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.
Full textVerma, 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.
Full textCheba, 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.
Full textConference papers on the topic "Xylanolytic and chitinolytic enzymes"
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.
Full textReports on the topic "Xylanolytic and chitinolytic enzymes"
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.
Full textHarman, 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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