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Journal articles on the topic 'Xylanolytic and chitinolytic enzymes'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Curotto, E., C. Aguirre, M. Concha, A. Nazal, V. Campos, E. Esposito, R. Angelo, A. M. F. Milagres, and N. Duran. "New methodology for fungal screening: Xylanolytic enzymes." Biotechnology Techniques 7, no. 11 (October 1993): 821–22. http://dx.doi.org/10.1007/bf00153752.

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12

Lindner, C., J. Stulke, and M. Hecker. "Regulation of xylanolytic enzymes in Bacillus subtilis." Microbiology 140, no. 4 (April 1, 1994): 753–57. http://dx.doi.org/10.1099/00221287-140-4-753.

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13

Sharma, Reetika, Gurvinder Singh Kocher, Ravinder Singh Bhogal, and Harinder Singh Oberoi. "Cellulolytic and xylanolytic enzymes from thermophilicAspergillus terreusRWY." Journal of Basic Microbiology 54, no. 12 (July 22, 2014): 1367–77. http://dx.doi.org/10.1002/jobm.201400187.

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14

Terrasan, César Rafael Fanchini, Beatriz Temer, Marta Cristina Teixeira Duarte, and Eleonora Cano Carmona. "Production of xylanolytic enzymes by Penicillium janczewskii." Bioresource Technology 101, no. 11 (June 2010): 4139–43. http://dx.doi.org/10.1016/j.biortech.2010.01.011.

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15

Chmielnicka, Jadwiga, Henryk Młodecki, and Maria Trocha. "Chitinolytic enzymes (chitinase and chitobiase) in mushrooms." Acta Mycologica 6, no. 2 (November 21, 2014): 315–23. http://dx.doi.org/10.5586/am.1970.019.

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16

Hodge, Angela, Ian J. Alexander, and Graham W. Gooday. "Chitinolytic enzymes of pathogenic and ectomycorrhizal fungi." Mycological Research 99, no. 8 (August 1995): 935–41. http://dx.doi.org/10.1016/s0953-7562(09)80752-1.

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17

Dahiya, Neetu, Rupinder Tewari, and Gurinder Singh Hoondal. "Biotechnological aspects of chitinolytic enzymes: a review." Applied Microbiology and Biotechnology 71, no. 6 (July 21, 2006): 773–82. http://dx.doi.org/10.1007/s00253-005-0183-7.

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18

Gohel, V., and D. C. Naseby. "Thermalstabilization of chitinolytic enzymes of Pantoea dispersa." Biochemical Engineering Journal 35, no. 2 (July 2007): 150–57. http://dx.doi.org/10.1016/j.bej.2007.01.009.

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19

Kopečný, J., and B. Hodrová. "Chitinolytic enzymes produced by ovine rumen bacteria." Folia Microbiologica 45, no. 5 (October 2000): 465–68. http://dx.doi.org/10.1007/bf02817622.

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20

Ontañon, Ornella M., Soma Bedő, Silvina Ghio, Mercedes M. Garrido, Juliana Topalian, Dóra Jahola, Anikó Fehér, Maria Pia Valacco, Eleonora Campos, and Csaba Fehér. "Optimisation of xylanases production by two Cellulomonas strains and their use for biomass deconstruction." Applied Microbiology and Biotechnology 105, no. 11 (May 21, 2021): 4577–88. http://dx.doi.org/10.1007/s00253-021-11305-y.

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Abstract One of the main distinguishing features of bacteria belonging to the Cellulomonas genus is their ability to secrete multiple polysaccharide degrading enzymes. However, their application in biomass deconstruction still constitutes a challenge. We addressed the optimisation of the xylanolytic activities in extracellular enzymatic extracts of Cellulomonas sp. B6 and Cellulomonas fimi B-402 for their subsequent application in lignocellulosic biomass hydrolysis by culture in several substrates. As demonstrated by secretomic profiling, wheat bran and waste paper resulted to be suitable inducers for the secretion of xylanases of Cellulomonas sp. B6 and C. fimi B-402, respectively. Both strains showed high xylanolytic activity in culture supernatant although Cellulomonas sp. B6 was the most efficient xylanolytic strain. Upscaling from flasks to fermentation in a bench scale bioreactor resulted in equivalent production of extracellular xylanolytic enzymatic extracts and freeze drying was a successful method for concentration and conservation of the extracellular enzymes, retaining 80% activity. Moreover, enzymatic cocktails composed of combined extra and intracellular extracts effectively hydrolysed the hemicellulose fraction of extruded barley straw into xylose and xylooligosaccharides. Key points • Secreted xylanase activity of Cellulomonas sp. B6 and C. fimi was maximised. • Biomass-induced extracellular enzymes were identified by proteomic profiling. • Combinations of extra and intracellular extracts were used for barley straw hydrolysis.

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21

Rohman, Ali, Bauke W. Dijkstra, and Ni Nyoman Tri Puspaningsih. "β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides." International Journal of Molecular Sciences 20, no. 22 (November 6, 2019): 5524. http://dx.doi.org/10.3390/ijms20225524.

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Xylan, a prominent component of cellulosic biomass, has a high potential for degradation into reducing sugars, and subsequent conversion into bioethanol. This process requires a range of xylanolytic enzymes. Among them, β-xylosidases are crucial, because they hydrolyze more glycosidic bonds than any of the other xylanolytic enzymes. They also enhance the efficiency of the process by degrading xylooligosaccharides, which are potent inhibitors of other hemicellulose-/xylan-converting enzymes. On the other hand, the β-xylosidase itself is also inhibited by monosaccharides that may be generated in high concentrations during the saccharification process. Structurally, β-xylosidases are diverse enzymes with different substrate specificities and enzyme mechanisms. Here, we review the structural diversity and catalytic mechanisms of β-xylosidases, and discuss their inhibition by monosaccharides.

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22

Chernin, Leonid, Aviva Gafni, Abraham Sztejnberg, Rita Mozes-Koch, and Uri Gerson. "Chitinolytic activity of the acaropathogenic fungiHirsutella thompsoniiandHirsutella necatrix." Canadian Journal of Microbiology 43, no. 5 (May 1, 1997): 440–46. http://dx.doi.org/10.1139/m97-062.

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Two isolates of the acaropathogenic fungus Hirsutella thompsonii (Nos. 255 and 414), and Hirsutella necatrix, were able to produce and excrete chitinolytic enzymes. A chitobiase of > 205 kDa was excreted by all fungi and a chitobiase of 112 kDa only by isolate 414. An endochitinase of 162 kDa was excreted by isolate 414 and two endochitinases of 66 and 38 kDa were excreted by isolate 255. Both H. thompsonii isolates produced chitinolytic enzymes only under inducible conditions, in the presence of colloidal chitin as the sole source of carbon. Hirsutella necatrix produced a chitobiase constitutively when grown in the presence of glucose. In addition to chitinolytic enzymes, the H. thompsonii isolates excreted proteolytic activities, including elastase, as well as α-esterase and α-amylase activities. Hirsutella necatrix was unable to use casein, milk powder, or elastin as the sole carbon source. The acaropathogenicity of these isolates was assayed on the carmine spider mite (Tetranychus cinnabarinus). Isolates 414 and 255 and H. necatrix killed ca. 80, 35, and 15%, respectively, of the infected mites. The role of chitinolytic and other enzymatic activities in the acaropathogenicity of these fungi is discussed.Key words: acaropathogenic fungi, Hirsutella, chitobiase, endochitinase, α-amylase.

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23

Zahovic, Ida, Zorana Roncevic, Jovana Grahovac, Sinisa Dodic, Aleksandar Jokic, and Jelena Dodic. "The effect of cultivation technique on enzymes production from sugar beet pulp by Neurospora crassa." Acta Periodica Technologica, no. 50 (2019): 338–45. http://dx.doi.org/10.2298/apt1950338z.

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This study is concerned with the effect of different cultivation techniques on enzymes production from sugar beet pulp by strain Neurospora crassa isolated from the environment. Cultivation of selected producing microorganism was carried out under the same process conditions using five techniques. Bioprocess efficacy was estimated based on amylolytic, cellulolytic and xylanolytic activity of prepared enzymes mixtures. The obtained results indicate that the selection of cultivation technique had a statistically significant effect on the production of examined hydrolytic enzymes. It was confirmed that solid state cultivation with spontaneous aeration is the best cultivation technique for the production of amylolytic, cellulolytic and xylanolytic enzymes from sugar beet pulp by Neurospora crassa. Submerged cultivation of producing strain with spontaneous aeration resulted in the lowest production of all investigated enzymes under applied experimental conditions. The obtained results are the basis for further research aimed to increase the enzymes yield and activity of their mixture.

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24

Ito, Kiyoshi. "Gene Family of the Xylanolytic Enzymes of Fungi." Nippon Nōgeikagaku Kaishi 69, no. 3 (1995): 362–64. http://dx.doi.org/10.1271/nogeikagaku1924.69.362.

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25

Teunissen, Marcel J., and Huub J. M. Op den Camp. "Anaerobic fungi and their cellulolytic and xylanolytic enzymes." Antonie van Leeuwenhoek 63, no. 1 (January 1993): 63–76. http://dx.doi.org/10.1007/bf00871733.

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26

Biely, Peter, and Vladimír Puchart. "Recent progress in the assays of xylanolytic enzymes." Journal of the Science of Food and Agriculture 86, no. 11 (2006): 1636–47. http://dx.doi.org/10.1002/jsfa.2519.

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27

Rahman, A. K. M. Shofiqur, Naoyasu Sugitani, Masahiro Hatsu, and Kazuhiro Takamizawa. "A role of xylanase, α-L-arabinofuranosidase, and xylosidase in xylan degradation." Canadian Journal of Microbiology 49, no. 1 (January 1, 2003): 58–64. http://dx.doi.org/10.1139/w02-114.

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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 oatspelt xylan was investigated. Optimum production of the enzymes was found in culture containing oatspelt 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 oatspelt 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.

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28

Ruthes, Andrea C., Antonio Martínez-Abad, Hwei-Ting Tan, Vincent Bulone, and Francisco Vilaplana. "Sequential fractionation of feruloylated hemicelluloses and oligosaccharides from wheat bran using subcritical water and xylanolytic enzymes." Green Chemistry 19, no. 8 (2017): 1919–31. http://dx.doi.org/10.1039/c6gc03473j.

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29

Fukamizo, Fukamizo. "Chitinolytic Enzymes: Catalysis, Substrate Binding, and their Application." Current Protein & Peptide Science 1, no. 1 (July 1, 2000): 105–24. http://dx.doi.org/10.2174/1389203003381450.

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30

MATSUMIYA, MASAHIRO, KOUJI MIYAUCHI, and ATSUSHI MOCHIZUKI. "Characterization and application of chitinolytic enzymes of squid." Fisheries science 68, sup2 (2002): 1579–82. http://dx.doi.org/10.2331/fishsci.68.sup2_1579.

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31

Broadway, Roxanne M., D. L. Williams, Wendy C. Kain, G. E. Harman, M. Lorito, and D. P. Labeda. "Partial characterization of chitinolytic enzymes from Streptomyces albidoflavus." Letters in Applied Microbiology 20, no. 5 (May 1995): 271–76. http://dx.doi.org/10.1111/j.1472-765x.1995.tb00444.x.

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32

Kumar, Sanjeev, Rohit Sharma, and Rupinder Tewari. "Production of N-Acetylglucosamine Using Recombinant Chitinolytic Enzymes." Indian Journal of Microbiology 51, no. 3 (January 30, 2011): 319–25. http://dx.doi.org/10.1007/s12088-011-0157-7.

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33

Šimůnek, J., G. Tishchenko, K. Rozhetsky, H. Bartoňová, J. Kopečný, and B. Hodrová. "Chitinolytic enzymes fromClostridium aminovalericum: Activity screening and purification." Folia Microbiologica 49, no. 2 (March 2004): 194–98. http://dx.doi.org/10.1007/bf02931401.

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34

Lacombe-Harvey, Marie-Ève, Ryszard Brzezinski, and Carole Beaulieu. "Chitinolytic functions in actinobacteria: ecology, enzymes, and evolution." Applied Microbiology and Biotechnology 102, no. 17 (June 21, 2018): 7219–30. http://dx.doi.org/10.1007/s00253-018-9149-4.

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35

Miltko, R., G. Belzecki, and T. Michalowski. "Chitinolytic enzymes of the rumen ciliate Eudiplodinium maggii." Folia Microbiologica 57, no. 4 (April 13, 2012): 317–19. http://dx.doi.org/10.1007/s12223-012-0133-6.

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36

Havukkala, I., C. Mitamura, S. Hara, K. Hirayae, Y. Nishizawa, and T. Hibi. "Induction and Purification of Beauveria bassiana Chitinolytic Enzymes." Journal of Invertebrate Pathology 61, no. 1 (January 1993): 97–102. http://dx.doi.org/10.1006/jipa.1993.1017.

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37

Kidibule, Peter E., Jessica Costa, Andrea Atrei, Francisco J. Plou, Maria Fernandez-Lobato, and Rebecca Pogni. "Production and characterization of chitooligosaccharides by the fungal chitinase Chit42 immobilized on magnetic nanoparticles and chitosan beads: selectivity, specificity and improved operational utility." RSC Advances 11, no. 10 (2021): 5529–36. http://dx.doi.org/10.1039/d0ra10409d.

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38

St Leger, R. J., R. M. Cooper, and A. K. Charnley. "Cuticle-degrading Enzymes of Entomopathogenic Fungi: Regulation of Production of Chitinolytic Enzymes." Microbiology 132, no. 6 (June 1, 1986): 1509–17. http://dx.doi.org/10.1099/00221287-132-6-1509.

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39

Ribeiro, Liliane Fraga Costa, Marcelo Gomes Marçal Vieira Vaz, Virgínia Maria Chaves-Alves, Maria Cristina Dantas Vanetti, Maria Catarina Megumi Kasuya, Flávia Maria Lopes Passos, and Antônio Galvão do Nascimento. "Thermostability of xylanolytic enzymes produced by Lentinula edodes UFV70." Brazilian Journal of Microbiology 43, no. 1 (March 2012): 201–4. http://dx.doi.org/10.1590/s1517-83822012000100021.

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40

Ferreira, GisÃ©lia, Cinthia G. Boer, and Rosane M. Peralta. "Production of xylanolytic enzymes byAspergillus tamariiin solid state fermentation." FEMS Microbiology Letters 173, no. 2 (April 1999): 335–39. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13522.x.

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41

Horvath-Szanics, E., J. Perjéssy, A. Klupács, K. Takács, A. Nagy, E. Koppány-Szabó, F. Hegyi, et al. "STUDY OF CHITINASE AND CHITINOLYTIC ACTIVITY OF LACTOBACILLUS STRAINS." Acta Alimentaria 49, no. 2 (June 2020): 214–24. http://dx.doi.org/10.1556/066.2020.49.2.11.

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The increasing consumer demand for less processed and more natural food products – while improving those products’ quality, safety, and shelf-life – has raised the necessity of chemical preservative replacement. Biopreservation refers to extended storage life and enhanced safety of foods using the natural microflora and (or) their antibacterial products. Chitinolytic enzymes are of biotechnological interest, since their substrate, chitin, is a major structural component of the cell wall of fungi, which are the main cause of the spoilage of food and raw plant material. Among the several organisms, many bacteria produce chitinolytic enzymes, however, this behaviour is not general. The chitinase activity of the lactic acid bacteria is scarcely known and studied.The aim of the present study was to select Lactobacillus strains that have genes encoding chitinase, furthermore, to detect expressed enzymes and to characterise their chitinase activity. Taking into consideration the importance of chitin-bindig proteins (CBPs) in the chitinase activity, CBPs were also examined. Five Lactobacillus strains out of 43 strains from 12 different species were selected by their chitinase coding gene. The presence of the chitinase and chitin-biding protein production were confirmed, however, no chitinolytic activity has been identified.

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42

Nampally, Malathi, M. B. Govinda Rajulu, Dominique Gillet, T. S. Suryanarayanan, and Bruno B. Moerschbacher. "A High Diversity in Chitinolytic and Chitosanolytic Species and Enzymes and Their Oligomeric Products Exist in Soil with a History of Chitin and Chitosan Exposure." BioMed Research International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/857639.

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Chitin is one of the most abundant biomolecules on earth, and its partially de-N-acetylated counterpart, chitosan, is one of the most promising biotechnological resources due to its diversity in structure and function. Recently, chitin and chitosan modifying enzymes (CCMEs) have gained increasing interest as tools to engineer chitosans with specific functions and reliable performance in biotechnological and biomedical applications. In a search for novel CCME, we isolated chitinolytic and chitosanolytic microorganisms from soils with more than ten-years history of chitin and chitosan exposure and screened them for chitinase and chitosanase isoenzymes as well as for their patterns of oligomeric products by incubating their secretomes with chitosan polymers. Of the 60 bacterial strains isolated, only eight were chitinolytic and/or chitosanolytic, while 20 out of 25 fungal isolates were chitinolytic and/or chitosanolytic. The bacterial isolates produced rather similar patterns of chitinolytic and chitosanolytic enzymes, while the fungal isolates produced a much broader range of different isoenzymes. Furthermore, diverse mixtures of oligosaccharides were formed when chitosan polymers were incubated with the secretomes of select fungal species. Our study indicates that soils with a history of chitin and chitosan exposure are a good source of novel CCME for chitosan bioengineering.

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43

van Peij, Noël N. M. E., Marco M. C. Gielkens, Ronald P. de Vries, Jaap Visser, and Leo H. de Graaff. "The Transcriptional Activator XlnR Regulates Both Xylanolytic and Endoglucanase Gene Expression inAspergillus niger." Applied and Environmental Microbiology 64, no. 10 (October 1, 1998): 3615–19. http://dx.doi.org/10.1128/aem.64.10.3615-3619.1998.

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ABSTRACT The expression of genes encoding enzymes involved in xylan degradation and two endoglucanases involved in cellulose degradation was studied at the mRNA level in the filamentous fungusAspergillus niger. A strain with a loss-of-function mutation in the xlnR gene encoding the transcriptional activator XlnR and a strain with multiple copies of this gene were investigated in order to define which genes are controlled by XlnR. The data presented in this paper show that the transcriptional activator XlnR regulates the transcription of thexlnB, xlnC, and xlnD genes encoding the main xylanolytic enzymes (endoxylanases B and C and β-xylosidase, respectively). Also, the transcription of the genes encoding the accessory enzymes involved in xylan degradation, including α-glucuronidase A, acetylxylan esterase A, arabinoxylan arabinofuranohydrolase A, and feruloyl esterase A, was found to be controlled by XlnR. In addition, XlnR also activates transcription of two endoglucanase-encoding genes, eglA andeglB, indicating that transcriptional regulation by XlnR goes beyond the genes encoding xylanolytic enzymes and includes regulation of two endoglucanase-encoding genes.

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44

Poria, Vikram, Anuj Rana, Arti Kumari, Jasneet Grewal, Kumar Pranaw, and Surender Singh. "Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications." Biology 10, no. 12 (December 12, 2021): 1319. http://dx.doi.org/10.3390/biology10121319.

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Chitinases are a large and diversified category of enzymes that break down chitin, the world’s second most prevalent polymer after cellulose. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase (GH) families. Most of the distinct GH families, as well as the unique structural and catalytic features of various chitinolytic enzymes, have been thoroughly explored to demonstrate their use in the development of tailor-made chitinases by protein engineering. Although chitin-degrading enzymes may be found in plants and other organisms, such as arthropods, mollusks, protozoans, and nematodes, microbial chitinases are a promising and sustainable option for industrial production. Despite this, the inducible nature, low titer, high production expenses, and susceptibility to severe environments are barriers to upscaling microbial chitinase production. The goal of this study is to address all of the elements that influence microbial fermentation for chitinase production, as well as the purifying procedures for attaining high-quality yield and purity.

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45

Koga, Daizo, Nobuyuki Sueshige, Kazuhiko Orikono, Toshihiko Utsumi, Shuhei Tanaka, Yoshio Yamada, and Akio Ide. "Efficiency of Chitinolytic Enzymes in the Formation ofTricholoma matsutakeProtoplasts." Agricultural and Biological Chemistry 52, no. 8 (August 1988): 2091–93. http://dx.doi.org/10.1080/00021369.1988.10868973.

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46

Harman, G. E. "Chitinolytic Enzymes ofTrichoderma harzianum: Purification of Chitobiosidase and Endochitinase." Phytopathology 83, no. 3 (1993): 313. http://dx.doi.org/10.1094/phyto-83-313.

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47

Lorito, M. "Antifungal, Synergistic Interaction Between Chitinolytic Enzymes fromTrichoderma harzianumandEnterobacter cloacae." Phytopathology 83, no. 9 (1993): 721. http://dx.doi.org/10.1094/phyto-83-721.

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48

Huang, J. H., C. J. Chen, and Y. C. Su. "Production of chitinolytic enzymes from a novel species ofAeromonas." Journal of Industrial Microbiology 17, no. 2 (August 1996): 89–95. http://dx.doi.org/10.1007/bf01570049.

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Ferreira, L., F. Moscoso, M. C. Sieiro, M. A. Sanromán, and M. A. Longo. "Development of novel microbial systems for chitinolytic enzymes production." New Biotechnology 29 (September 2012): S109. http://dx.doi.org/10.1016/j.nbt.2012.08.306.

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Tews, Ivo, Anke C. Terwisscha van Scheltinga, Anastassis Perrakis, Keith S. Wilson, and Bauke W. Dijkstra. "Substrate-Assisted Catalysis Unifies Two Families of Chitinolytic Enzymes." Journal of the American Chemical Society 119, no. 34 (August 1997): 7954–59. http://dx.doi.org/10.1021/ja970674i.

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