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Статті в журналах з теми "Endo-(1,4)-β-glucanase"

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Автор: Grafiati

Опубліковано: 10 грудня 2022

Оновлено: 28 січня 2023

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1

Fujiwara, Takaaki, Ayumi Fujishima, Yui Nakamura, Kenji Tajima та Min Yao. "Structural snapshot of a glycoside hydrolase family 8 endo-β-1,4-glucanase capturing the state after cleavage of the scissile bond". Acta Crystallographica Section D Structural Biology 78, № 2 (24 січня 2022): 228–37. http://dx.doi.org/10.1107/s2059798321012882.

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Bacterial cellulose (BC), which is produced by bacteria, is a biodegradable and biocompatible natural resource. Because of its remarkable physicochemical properties, BC has attracted attention for the development and manufacture of biomedical and industrial materials. In the BC production system, the enzyme endo-β-1,4-glucanase, which belongs to glycoside hydrolase family 8 (GH8), acts as a cleaner by trimming disordered cellulose fibers to produce high-quality BC. Understanding the molecular mechanism of the endo-β-1,4-glucanase would help in developing a reasonable biosynthesis of BC. Nevertheless, all of the steps in the reaction of this endo-β-1,4-glucanase are not clear. This study confirms the BC hydrolytic activity of the endo-β-1,4-glucanase from the BC-producing bacterium Enterobacter sp. CJF-002 (EbBcsZ) and reports crystal structures of EbBcsZ. Unlike in previously reported GH8 endo-β-1,4-glucanase structures, here the base catalyst was mutated (D242A) and the structure of this mutant bound to cellooligosaccharide [EbBcsZ(D242A)CPT] was analyzed. The EbBcsZ(D242A)CPT structure showed two cellooligosaccharides individually bound to the plus and minus subsites of EbBcsZ. The glucosyl unit in subsite −1 presented a distorted 5 S 1 conformation, a novel snapshot of a state immediately after scissile-bond cleavage. In combination with previous studies, the reaction process of endo-β-1,4-glucanase is described and the β-1,4-glucan-trimming mechanism of EbBcsZ is proposed. The EbBcsZ(D242A)CPT structure also showed an additional β-1,4-glucan binding site on the EbBcsZ surface, which may help to accept the substrate.

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2

Allardyce, Benjamin J., та Stuart M. Linton. "Synergistic interaction of an endo-β-1,4-glucanase and a β-glucohydrolase leads to more efficient hydrolysis of cellulose-like polymers in the gecarcinid land crab, Gecarcoidea natalis". Australian Journal of Zoology 60, № 5 (2012): 299. http://dx.doi.org/10.1071/zo12074.

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Анотація:

This study investigated synergism between endo-β-1,4-glucanase and β-glucohydrolase enzymes from Gecarcoidea natalis. Together, these enzymes efficiently hydrolyse the cellulose-like polymer, carboxymethyl cellulose, to glucose. Endo-β-1,4-glucanase and β-glucohydrolase, isolated previously from G. natalis, were incubated in vitro using a ratio of the measured activities that matches that found in their digestive juice (5.4 : 1). Their combined activity, measured as the release of glucose from carboxymethyl cellulose, was greater than the sum of their separate activities. Hence they synergistically released glucose from carboxymethyl cellulose (degree of synergy: 1.27). This may be due to the complementary nature of the products of endo-β-1,4-glucanase activity and the preferred substrates of the β-glucohydrolase. β-glucohydrolase may also enhance cellulose hydrolysis by removing cellobiose, a potential competitive inhibitor of endo-β-1,4-glucanase. The synergistic interaction of these two enzymes further supports the previous suggestion that this species possesses a novel two-enzyme cellulase system that differs from the traditional three-enzyme fungal model.

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3

Ya. V., Chabaniuk, Brovko I. S., Melnikova I. O. та Spataru K. V. "SEARCHING ENDO-1,4-β-GLUCANASE ACTIVE PRODUCERS FOR BIODESTRUCTION OF PLANT RESIDUES". Agriciltural microbiology 34 (11 листопада 2021): 15–22. http://dx.doi.org/10.35868/1997-3004.34.15-22.

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Анотація:

Objective. Evaluate the activity of endo-1,4-β-glucanase in soil microorganisms Bacillus subtilis, Paenibacillus polymyxa, Chaetomium globosum and Trichoderma harzianum for their potential use as an enzyme source in biotechnological production and to create a biodestroyer of plant residues. Methods. Hole method based on the interaction between Congo red dye and polysaccharide containing β (1.4) or β (1.3) bonds (mannitol-yeast medium was applied for deep cultivation of B. subtilis and P. polymyxa, corn-molasses — for C. globosum and T. harzianum), and spectrophotometric method based on colorimetric determination of the optical density of ferricyanide solution, the excess of which remains after reaction with reducing substances present in the culture fluid (microorganisms were cultured on corn-molasses medium). Results. Both hole and spectrophotometric methods showed that the studied micromycete strains had higher endo-1,4-β-glucanase activity than bacterial strains. The activity of endo-1,4-β-glucanase of microorganisms is as follows: B. subtilis eko/206 — 0.0499 IU/ml, T. harzianum eko/101 — 0.0667 IU/ml; C. globosum eko/108 — 0.0673 IU/ml. The average diameters of the enlightenment zones are as follows: T. harzianum eko/101 — 27.00 mm; C. globosum eko/108 — 28.14 mm; B. subtilis eko/206 — 20.25 mm. No endoglucanase activity was detected in P. polymyxa eko/204. Conclusion. The study of endo-1,4-β- glucanase activity in strains of microorganisms showed that the highest enzymatic activity is observed in C. globosum eko/108 and T. harzianum eko/101, suggesting the prospects of using these strains to obtain endo-1,4-β-glucanase via biotechnology. Although B. subtilis eko/206 has the ability to produce cellulolytic enzymes but their number is relatively small, so its use as a producer of endo-1,4-β-glucanase is less appropriate. P. polymyxa eko/204 did not show endoglucanase activity.

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4

Mendu, Lavanya, Gayani Jalathge, Kamalpreet Kaur Dhillon, Nagendra Pratap Singh, Vimal Kumar Balasubramanian, Rebecca Fewou, Dennis C. Gitz, Junping Chen, Zhanguo Xin та Venugopal Mendu. "Mutation in the Endo-β-1,4-glucanase (KORRIGAN) Is Responsible for Thick Leaf Phenotype in Sorghum". Plants 11, № 24 (15 грудня 2022): 3531. http://dx.doi.org/10.3390/plants11243531.

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Sorghum [Sorghum bicolor (L.) Moench] is an important crop for food, feed, and fuel production. Particularly, sorghum is targeted for cellulosic ethanol production. Extraction of cellulose from cell walls is a key process in cellulosic ethanol production, and understanding the components involved in cellulose synthesis is important for both fundamental and applied research. Despite the significance in the biofuel industry, the genes involved in sorghum cell wall biosynthesis, modification, and degradation have not been characterized. In this study, we have identified and characterized three allelic thick leaf mutants (thl1, thl2, and thl3). Bulked Segregant Analysis sequencing (BSAseq) showed that the causal mutation for the thl phenotype is in endo-1,4-β-glucanase gene (SbKOR1). Consistent with the causal gene function, the thl mutants showed decreased crystalline cellulose content in the stem tissues. The SbKOR1 function was characterized using Arabidopsis endo-1,4-β-glucanase gene mutant (rsw2-1). Complementation of Arabidopsis with SbKOR1 (native Arabidopsis promoter and overexpression by 35S promoter) restored the radial swelling phenotype of rsw2-1 mutant, proving that SbKOR1 functions as endo-1,4-β-glucanase. Overall, the present study has identified and characterized sorghum endo-1,4-β-glucanase gene function, laying the foundation for future research on cell wall biosynthesis and engineering of sorghum for biofuel production.

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5

Mwenje, E., and N. Mguni. "Cellulolytic and pectinolytic activities of Capnodium isolates (sooty mould) from Zimbabwe." Canadian Journal of Botany 79, no. 12 (December 1, 2001): 1492–95. http://dx.doi.org/10.1139/b01-126.

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The cellulolytic and pectinolytic activities of five Capnodium (sooty mould) isolates previously associated with preharvest spoilage of avocado (Persea americana Mill.) fruits in Zimbabwe were assessed in liquid culture and in artificially infected avocado fruits. Polygalacturonase, endo-1,4-β-glucanase, and exo-1,4-β-glucanase activities were determined by measuring the increase in reducing groups using the dinitrosalicylic acid method, while for pectin lyase activity the thiobarbituric acid method was used. The five isolates showed the ability to produce polygalacturonase, pectin lyase, and endo-1,4-β-glucanase enzymes. Exo-1,4-β-glucanase activity was only detected in infected avocado tissue. The greyish black Capnodium isolates (Av7, Av8, and Av12) belonging to group I showed higher polygalacturonase and pectin lyase activities in both liquid culture and infected fruits than isolates Av3 and Av10 from group II. The same isolates showed higher exo-1,4-β-glucanase activity in infected avocado fruits. Results indicate that Capnodium, which normally is nonpathogenic, secretes cell wall degrading enzymes, especially pectic and cellulase enzymes. The detection of these enzymes in inoculated avocado fruits suggests a possible role in the preharvest soft rot of avocado fruits caused by Capnodium in Zimbabwe.Key words: Capnodium, sooty mould, pectic enzymes, avocados, cellulases.

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6

Zerva, Ioanna, Nikolaos Remmas, and Spyridon Ntougias. "Biocatalyst Potential of Cellulose-Degrading Microorganisms Isolated from Orange Juice Processing Waste." Beverages 5, no. 1 (March 2, 2019): 21. http://dx.doi.org/10.3390/beverages5010021.

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Cellulases can be applied as macerating and peeling enzymes in the orange juice processing industry. In this work, indigenous cellulose-degrading microorganisms were isolated from orange juice processing waste through successive enrichment procedures using carboxymethyl cellulose (CMC) as the sole carbon source. A total of 24 microbial isolates were screened for their ability to grow in CMC liquid medium, resulting in the selection of seven isolates. The latter were further assessed by determining their endo-1,4-β-d-glucanase, exo-1,4-β-d-glucanase, and β-1,4-d-glucosidase activities, of which their respective activities were as high as 3.89, 10.67, and 10.69 U/mg protein. All cellulose-degraders selected belonged to the genus Paenibacillus, although to distinct operational taxonomic units related to P. xylanexedens, P. tundrae, and P. pabuli (operational taxonomic unit—OTU#1) and to P. wynnii, P. odorifer, and P. donghaensis (OTU#2) spectrum. Regarding the cellulase activities of the orange juice processing waste, endo-1,4-β-d-glucanase activity (4.00 ± 0.11 U/g) was exerted only extracellularly, whereas exo-1,4-β-d-glucanase (2.60 ± 0.19 U/g) and β-1,4-d-glucosidase (5.69 ± 0.23 U/g) activities were exhibited both extracellularly and intracellularly. In conclusion, orange juice processing waste can be considered as a valuable source for the isolation of cellulose-degrading microbiota with potential uses in beverage industry, solid state fermentation and energy production.

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7

Allardyce, Benjamin J., and Stuart M. Linton. "Characterisation of cellulose and hemicellulose digestion in land crabs with special reference to Gecarcoidea natalis." Australian Journal of Zoology 59, no. 6 (2011): 380. http://dx.doi.org/10.1071/zo11054.

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This article reviews the current knowledge of cellulose and hemicellulose digestion by herbivorous land crabs using the gecarcinid Gecarcoidea natalis as a model species for this group. Cellulose digestion in the gecarcinids is hypothesised to require mechanical fragmentation and enzymatic hydrolysis. Mechanical fragmentation is achieved by the chelae, mandibles and gastric mill, which reduce the material to particles less than 53 µm. The gastric mill shows adaptations towards a plant diet; in particular, there are transverse ridges on the medial and lateral teeth and ventral cusps on the lateral teeth that complement and interlock to provide efficient cutting surfaces. Enzymatic hydrolysis of cellulose and hemicellulose is achieved through cellulase and hemicellulase enzymes. In the gecarcinids, 2–3 endo-β-1,4-glucanases, one β-glucohydrolase and a laminarinase have been identified. The endo-β-1,4-glucanases are multifunctional, with both endo-β-1,4-glucanase and lichenase activity. Complete cellulose hydrolysis is achieved through the synergistic action of the endo-β-1,4-glucanase and β-glucohydrolase. The evidence for the endogenous production of the cellulase and hemicellulase enzymes, their evolutionary origin and possible evolution in invertebrates as they colonised land is also discussed.

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8

Han, Yejun, Dylan Dodd, Charles W. Hespen, Samuel Ohene-Adjei, Charles M. Schroeder, Roderick I. Mackie та Isaac K. O. Cann. "Comparative Analyses of Two Thermophilic Enzymes Exhibiting both β-1,4 Mannosidic and β-1,4 Glucosidic Cleavage Activities from Caldanaerobius polysaccharolyticus". Journal of Bacteriology 192, № 16 (18 червня 2010): 4111–21. http://dx.doi.org/10.1128/jb.00257-10.

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ABSTRACT The hydrolysis of polysaccharides containing mannan requires endo-1,4-β-mannanase and 1,4-β-mannosidase activities. In the current report, the biochemical properties of two endo-β-1,4-mannanases (Man5A and Man5B) from Caldanaerobius polysaccharolyticus were studied. Man5A is composed of an N-terminal signal peptide (SP), a catalytic domain, two carbohydrate-binding modules (CBMs), and three surface layer homology (SLH) repeats, whereas Man5B lacks the SP, CBMs, and SLH repeats. To gain insights into how the two glycoside hydrolase family 5 (GH5) enzymes may aid the bacterium in energy acquisition and also the potential application of the two enzymes in the biofuel industry, two derivatives of Man5A (Man5A-TM1 [TM1 stands for truncational mutant 1], which lacks the SP and SLH repeats, and Man5A-TM2, which lacks the SP, CBMs, and SLH repeats) and the wild-type Man5B were biochemically analyzed. The Man5A derivatives displayed endo-1,4-β-mannanase and endo-1,4-β-glucanase activities and hydrolyzed oligosaccharides with a degree of polymerization (DP) of 4 or higher. Man5B exhibited endo-1,4-β-mannanase activity and little endo-1,4-β-glucanase activity; however, this enzyme also exhibited 1,4-β-mannosidase and cellodextrinase activities. Man5A-TM1, compared to either Man5A-TM2 or Man5B, had higher catalytic activity with soluble and insoluble polysaccharides, indicating that the CBMs enhance catalysis of Man5A. Furthermore, Man5A-TM1 acted synergistically with Man5B in the hydrolysis of β-mannan and carboxymethyl cellulose. The versatility of the two enzymes, therefore, makes them a resource for depolymerization of mannan-containing polysaccharides in the biofuel industry. Furthermore, on the basis of the biochemical and genomic data, a molecular mechanism for utilization of mannan-containing nutrients by C. polysaccharolyticus is proposed.

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9

Zheng, Baisong, Wen Yang, Xinyu Zhao, Yuguo Wang, Zhiyong Lou, Zihe Rao та Yan Feng. "Crystal Structure of Hyperthermophilic Endo-β-1,4-glucanase". Journal of Biological Chemistry 287, № 11 (29 листопада 2011): 8336–46. http://dx.doi.org/10.1074/jbc.m111.266346.

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10

Touzani, Abdellah, and Bernard Donèche. "Production et propriétés du complexe cellulasique du Botrytis cinerea." Canadian Journal of Botany 74, no. 3 (March 1, 1996): 486–91. http://dx.doi.org/10.1139/b96-059.

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The production of cellulasic complex by the fungal pathogen Botrytis cinerea is induced by addition of cellulose in the culture medium. The amount of activity increases greatly when the culture medium is supplemented with pectins, whereas glucose and cellobiose strongly inhibit the production of the complex. The cellulasic complex is constituted by three enzymes, separated and identified as β-glucosidase, exo 1,4-β-D-glucanase and endo 1,4-β-D-glucanase. The catalytic activity of the whole cellulasic complex is low and the inhibitors glucose and cellobiose act differently on this activity. Keywords: fungal pathogen, Botrytis cinerea, cellulasic complex, β-glucosidase, 1,4-β-D-glucanases.

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11

Arimori, Takao, Akihiro Ito, Masami Nakazawa, Mitsuhiro Ueda та Taro Tamada. "Crystal structure of endo-1,4-β-glucanase fromEisenia fetida". Journal of Synchrotron Radiation 20, № 6 (1 жовтня 2013): 884–89. http://dx.doi.org/10.1107/s0909049513021110.

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12

Freire, S. "Production of endo-1,4-β-?-glucanase by Curvularia pallescens". Carbohydrate Polymers 39, № 1 (травень 1999): 61–65. http://dx.doi.org/10.1016/s0144-8617(98)00082-4.

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13

Wang, Xu, Liang Rong, Mingfu Wang, Yingjie Pan, Yong Zhao, and Fang Tao. "Improving the activity of endoglucanase I (EGI) from Saccharomyces cerevisiae by DNA shuffling." RSC Adv. 7, no. 73 (2017): 46246–56. http://dx.doi.org/10.1039/c6ra26508a.

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To enhance the endo-β-1,4-glucanase activity of three mixedTrichodermasp. (Trichoderma reesei, Trichoderma longibrachiatum, andTrichoderma pseudokoningii), we optimized the efficiency of the encoding gene using DNA shuffling andSaccharomyces cerevisiaeINVSc1 as a host.

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14

Agustini, Luciasih, Ragil S. B. Irianto, Maman Turjaman, Sarah Asih Faulina, Resti Ariantari, Sira Stephandra, Herni Yuniar, Aryanto Aryanto, Najmulah Najmulah, and Ahmad Yani. "PENGARUH KONDISI KULTUR PADA AKTIVITAS SELULASE ISOLAT Pycnoporus sp. DAN Phlebiopsis sp. (EFFECTS OF CULTURE CONDITIONS ON CELLULASE ACTIVITIES PRODUCED BY Pycnoporus sp. AND Phlebiopsis sp.)." JURNAL SELULOSA 7, no. 02 (December 30, 2017): 79. http://dx.doi.org/10.25269/jsel.v7i02.215.

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Анотація:

The effects of media, pH and temperature on cellulase-complex enzyme produced by Pycnoporus sp. FORDACC-03452 and Phlebiopsis sp. FORDACC-02482 cultivated in rice bran and corn cobs media under solid state fermentation with pH 4–7 and temperature 30°C–45°C were investigated. Rice bran media showed a propensity to induce endo-β,1,4-glucanase and cellobiohydrolase productions, while corn cobs media induce β-glucosidase production. However, the mixture of rice bran and corn cobs did not result in better cellulase complex enzyme activities. Cellulase-complex produced by Pycnoporussp. showed superior activities compared to those produced by Phlebiopsissp. Crude enzyme of Pycnoporus sp. showed optimum specifc-activities of endo-β-1,4-glucanase at pH 6, temperature 35°C (0.403 ± 0.010 IU/mg), cellobiohydrolase at pH 6, temperature 40°C (0.540 ± 0.020 IU/mg) and β-glucosidase at pH 4, temperature 30 °C (0.022 ± 0.001 IU/mg). While Phlebiopsis sp. showed optimum specifc-activities of endo-β-1,4-glucanase at pH 6, temperature 35°C (0.202 ± 0.005 IU/mg), cellobiohydrolase at pH 4, temperature 45°C (0.180 ± 0.002 IU/mg) and β-glucosidase at pH 6, temperature 45°C (0.007 ± 0.001 IU/mg). Due to low β-glucosidase activities, the cellulase-complex generated from this study were not able to completely hydrolyse lignocellulosic waste and yielded unsufficient sugars content. Further investigation to optimize cellulase-complex production from these fungal isolates is still required.ABSTRAKPenelitian pengaruh media kultivasi, pH dan suhu inkubasi terhadap produksi enzim selulase-kompleks dari Pycnoporus sp. FORDACC-03452 dan Phlebiopsis sp. FORDACC-02482 yang ditumbuhkan di media dedak padi dan tongkol jagung dengan metode kultur padat pada variasi pH 4–7 dan suhu 30°C–45°C, telah dilakukan. Hasil memperlihatkan bahwa media dedak padi cenderung menginduksi produksi endo-β-1,4-glukanase dan selobiohidrolase, sedangkan media tongkol jagung menginduksi produksi β-glukosidase. Namun, campuran kedua substrat tersebut tidak menghasilkan aktivitas selulase yang lebih baik. Selulase-kompleks yang dihasilkan Pycnoporus sp. menunjukkan aktivitas lebih baik dibandingkan dengan yang diproduksi Phlebiopsis sp. Filtrat kasar Pycnoporus sp. menunjukkan aktivitas-spesifk endo-β-1,4-glukanase optimum pada pH 6, suhu 35°C (0,403 ± 0,010 IU/mg); selobiohidrolase pada pH 6, suhu 40°C (0,540 ± 0,020 IU/mg); dan β -glukosidase pada pH 4, suhu 30°C (0,022±0,001 IU/mg). Sementara, Phlebiopsis sp. menunjukkan aktivitas-spesifk endo-β-1,4-glukanase optimum pada pH 6, suhu 35°C (0,202 ± 0,005 IU/mg); selobiohidrolase pada pH 4, suhu 45°C (0,180 ± 0,002 IU/mg); dan β-glukosidase pada pH 6, suhu 45°C (0,007 ± 0,001 IU/mg). Rendahnya aktivitas β-glukosidase menyebabkan selulase-kompleks dari penelitian ini belum dapat menghidrolisis limbah lignoselulosa dengan sempurna dan kadar glukosa yang diperoleh masih rendah. Oleh karena itu, optimasi produksi selulasekompleks dari Pycnoporus sp. dan Phlebiopsis sp. masih perlu diteliti lebih lanjut.

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15

McCleary, Barry V., David Mangan, Robin Daly, Sébastien Fort, Ruth Ivory та Niall McCormack. "Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase)". Carbohydrate Research 385 (лютий 2014): 9–17. http://dx.doi.org/10.1016/j.carres.2013.12.001.

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16

Eshel, Dani, Itay Miyara, Tong Ailing, Amos Dinoor, and Dov Prusky. "pH Regulates Endoglucanase Expression and Virulence of Alternaria alternata in Persimmon Fruit." Molecular Plant-Microbe Interactions® 15, no. 8 (August 2002): 774–79. http://dx.doi.org/10.1094/mpmi.2002.15.8.774.

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Анотація:

The phytopathogenic fungus Alternaria alternata produces one endo-1,4-β-glucanase, AaK1, which is an important factor in disease development in persimmon fruit. During growth of A. alternata in media containing acidified yeast extract or cell walls from persimmon fruit, the fungus secreted ammonia and raised the medium pH. A rise in media pH from 3.8 to 6.0 in the presence of cell walls induced the expression of AaK1, whereas a glucose-induced decline in pH to 2.5 repressed transcription and enzymatic production. Treatments with buffered solutions at pH 6.0 during growth of A. alternata in the presence of glucose derepressed AaK1 expression and endo-1,4-β-glucanase production and enhanced decay development on the fruit. The results suggest that conditions affecting environmental pH modulate gene expression of AaK1 and virulence of A. alternata in persimmon fruit.

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17

Goellner, Melissa, Xiaohong Wang та Eric L. Davis. "Endo-β-1,4-Glucanase Expression in Compatible Plant–Nematode Interactions". Plant Cell 13, № 10 (жовтень 2001): 2241–55. http://dx.doi.org/10.1105/tpc.010219.

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18

Bawa, S. "Inheritance of endo-β-1,4-glucanase production in Trichoderma reesei". FEMS Microbiology Letters 145, № 2 (1 грудня 1996): 195–99. http://dx.doi.org/10.1016/s0378-1097(96)00407-7.

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19

Messner, R. "Intracellular precursors of endo-β-1,4-glucanase in Trichoderma reesei". FEMS Microbiology Letters 50, № 2-3 (травень 1988): 227–32. http://dx.doi.org/10.1016/0378-1097(88)90277-7.

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20

Linton, Stuart M., Peter Greenaway та David W. Towle. "Endogenous production of endo-β-1,4-glucanase by decapod crustaceans". Journal of Comparative Physiology B 176, № 4 (12 січня 2006): 339–48. http://dx.doi.org/10.1007/s00360-005-0056-5.

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21

Prokop, Andreas, Peter Rapp та Fritz Wagner. "Production, purification, and characterization of an extracellular endo-β-1, 3-glucanase from a monokaryon of Schizophyllum commune ATCC 38548 defective in exo-β-1, 3-glucanase formation". Canadian Journal of Microbiology 40, № 1 (1 січня 1994): 18–23. http://dx.doi.org/10.1139/m94-003.

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Production of extracellular β-1, 3-glucanase activity by a monokaryotic Schizophyllum commune strain was monitored and results indicated that the β-glucanase activity consisted of an endo- β-1, 3-glucanase activity, besides a negligible amount of β-1, 6-glucanase and β-glucosidase activity. Unlike the β-1, 3-glucanase production of the dikaryotic parent strain S. commune ATCC 38548, the β-1, 3-glucanase formation of the monokaryon was not regulated by catabolite repression. The endo- β-1, 3-glucanase of the monokaryon was purified from the culture filtrate by lyophilization, anion exchange chromatography on Mono Q, and gel filtration on Sephacryl S-100. It appeared homogeneous on SDS-PAGE with a molecular mass of 35.5 kDa and the isoelectric point was 3.95. The enzyme was only active toward glucans containing β-1, 3-linkages, including lichenan, a β-1, 3-1, 4-D-glucan. It attacked laminarin in an endo-like fashion to form laminaribiose, laminaritriose, and high oligosaccharides. While the extracellular β-glucanases from the dikaryotic S. commune ATCC 38548 degraded significant amounts of schizophyllan, the endo- β-1, 3-glucanase from the monokaryon showed greatly reduced activity toward this high molecular mass β-1, 3-/β-1, 6-glucan. The Km of the endoglucanase, using laminarin as substrate, was 0.28 mg/mL. Optimal pH and temperature were 5.5 and 50 °C, respectively. The enzyme was stable between pH 5.5 and 7.0 and at temperatures below 50 °C. The enzyme was completely inhibited by 1 mM Hg2+. Growth of the monokaryotic S. commune strain was not affected by its constitutive endo- β-1, 3-glucanase formation.Key words: endo- β-1, 3-glucanase, Schizophyllum commune, monokaryon, constitutive endo- β-1, 3-glucanase formation.

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Valášková, Vendula, and Petr Baldrian. "Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus – production of extracellular enzymes and characterization of the major cellulases." Microbiology 152, no. 12 (December 1, 2006): 3613–22. http://dx.doi.org/10.1099/mic.0.29149-0.

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Piptoporus betulinus is a common wood-rotting fungus parasitic for birch (Betula species). It is able to cause fast mass loss of birch wood or other lignocellulose substrates. When grown on wheat straw, P. betulinus caused 65 % loss of dry mass within 98 days, and it produced endo-1,4-β-glucanase (EG), endo-1,4-β-xylanase, endo-1,4-β-mannanase, 1,4-β-glucosidase (BG), 1,4-β-xylosidase, 1,4-β-mannosidase and cellobiohydrolase activities. The fungus was not able to efficiently degrade crystalline cellulose. The major glycosyl hydrolases, endoglucanase EG1 and β-glucosidase BG1, were purified. EG1 was a protein of 62 kDa with a pI of 2.6–2.8. It cleaved cellulose internally, produced cellobiose and glucose from cellulose and cellooligosaccharides, and also showed β-xylosidase and endoxylanase activities. The K m for carboxymethylcellulose was 3.5 g l−1, with the highest activity at pH 3.5 and 70 °C. BG1 was a protein of 36 kDa with a pI around 2.6. It was able to produce glucose from cellobiose and cellooligosaccharides, but also produced galactose, mannose and xylose from the respective oligosaccharides and showed some cellobiohydrolase activity. The K m for p-nitrophenyl-1,4-β-glucoside was 1.8 mM, with the highest activity at pH 4 and 60 °C, and the enzyme was competitively inhibited by glucose (K i=5.8 mM). The fungus produced mainly β-glucosidase and β-mannosidase activity in its fruit bodies, while higher activities of endoglucanase, endoxylanase and β-xylosidase were found in fungus-colonized wood.

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23

Kim, Hoon, Dong Ho Ahn, Kyung Hwa Jung та Moo Young Pack. "Adsorption of Bacillus subtilis endo-β-1,4-glucanase to cellulosic materials". IUBMB Life 41, № 4 (квітень 1997): 665–77. http://dx.doi.org/10.1080/15216549700201711.

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24

Romaniec, M. P. M., K. Davidson, B. A. White та G. P. Hazlewood. "Cloning of Ruminococcus albus endo-β-1,4-glucanase and xylanase genes". Letters in Applied Microbiology 9, № 3 (вересень 1989): 101–4. http://dx.doi.org/10.1111/j.1472-765x.1989.tb00300.x.

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25

Tweddell, Russell J., Jennifer Marshall та Suha H. Jabaji-Hare. "Endo-1,4-β-glucanase production byStachybotrys elegans, a mycoparasite ofRhizoctonia solani". Mycologia 88, № 3 (травень 1996): 410–15. http://dx.doi.org/10.1080/00275514.1996.12026668.

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26

Mangan, D., B. V. McCleary, A. Liadova, R. Ivory та N. McCormack. "Quantitative fluorometric assay for the measurement of endo-1,4-β-glucanase". Carbohydrate Research 395 (серпень 2014): 47–51. http://dx.doi.org/10.1016/j.carres.2014.05.002.

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27

TAKEDA, Takumi, Fukumi SAKAI та Takahisa HAYASHI. "A Homologue ofEGL1Encoding Endo-1,4-β-glucanase in Elongating Pea Stems". Bioscience, Biotechnology, and Biochemistry 64, № 3 (січень 2000): 636–40. http://dx.doi.org/10.1271/bbb.64.636.

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28

Trainotti, L., L. Ferrarese та F. Dalla Vecchia. "Endo β-1,4-glucanase involvement in the abscission of pepper flowers". Giornale botanico italiano 130, № 4-6 (січень 1996): 971–72. http://dx.doi.org/10.1080/11263509609438379.

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29

Gordeeva, T. L., A. N. Kalinina, A. V. Serkina, A. S. Fedorov та S. P. Sineoky. "Expression of Gene for β-glucanase from Paenibacillus jamilae Bg1 in Pichia pastoris and Characteristics of Recombinant Enzyme". Biotekhnologiya 35, № 4 (2019): 15–23. http://dx.doi.org/10.21519/0234-2758-2019-35-4-15-23.

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The isolation, heterologous expression and characterization of a new thermostable β-glucanase from Paenibacillus jamilae is described. The bgl26 gene from the P. jamilae Bg1 VKPM B-13093 strain consisting of 714 nucleotides encodes endo-1,3-1,4-β-glucanase (EC 3.2.1.73) containing 213 amino acids and 24 residues of the putative signal peptide in N-end area. The nucleotide sequence of the bgl26 gene and the amino acid sequence of the mature Bgl26 protein have the greatest homology with the sequence of the Paenibacillus macerans endo-l,3-l,4-β-glucanase (82 and 88%, respectively). A fragment of the gene encoding the mature protein was expressed in Pichia pastoris. Purified recombinant enzyme Bgl26 was active towards barley β-glucan. The optimal pH for the enzyme to work was 7,0, and the optimum temperature range was 40-45 °C. The specific activity of β-glucanase was at the level of 6650 U/mg of protein, Km and Vmax were equal to 6.4 ± 0.3 mg/mL and 9450.1 ± 471.2 umol/(min-mg), respectively. The recombinant protein Bgl26 was characterized by high pH and thermal stability, as well as resistance to digestive enzymes. It is also shown that Co2+ ions have a positive effect on the activity of the enzyme. β-glucanase, β-glucan, Paenibacillus jamilae, Pichia pastoris The work was financially supported by the Ministry of Science and Higher Education of the Russian Federation (Unique Project Identifier RFMEFI60717X0179) and was carried out using the Multipurpose Scientific Installation of National Bio-Resource Center «All-Russian Collection of Industrial Microorganisms», NRC «Kurchatov Institute» - GOSNIIGENETIKA.

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30

Sharma, S. "Physical characterization of isozymes of endo-β-1,4-glucanase and β-1,4-glucosidase from Aspergillus species". FEMS Microbiology Letters 79, № 1 (15 березня 1991): 99–104. http://dx.doi.org/10.1016/0378-1097(91)90535-i.

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31

van Rensburg, Pierre, Willem H. van Zyl та Isak S. Pretorius. "Over-expression of the Saccharomyces cerevisiae exo-β-1,3-glucanase gene together with the Bacillus subtilis endo-β-1,3-1,4-glucanase gene and the Butyrivibrio fibrisolvens endo-β-1,4-glucanase gene in yeast". Journal of Biotechnology 55, № 1 (травень 1997): 43–53. http://dx.doi.org/10.1016/s0168-1656(97)00059-x.

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32

Melo, Thiago Anchieta de, Ilka Márcia Ribeiro de Souza Serra, and Ingrid Tayane Vieira da Silva do Nascimento. "Ascophyllum nodosum seaweed extract effect on morphology and cellulolytic ability of the fungus Fusarium oxysporum f. sp. vasinfectum." Research, Society and Development 9, no. 11 (November 19, 2020): e4079119913. http://dx.doi.org/10.33448/rsd-v9i11.9913.

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This work aimed to verify the effect in vitro, of Ascophyllum nodosum (AN) seaweed extract on the morphology and cellulolytic capacity of the fungus Fusarium oxysporum f. sp. vasinfectum (FOV). Thus, the fungus was placed in contact with different doses of the extract, being these: 0, 0.5, 1.0, 2.0, 4.0 and 8.0%. It was verified that the product, with increasing doses, progressively induced mycelial growth of the fungus, as measured by the diameter of the colonies and fresh mass of mycelium grown in PD (potato-dextrose) culture medium. This result was also corroborated by the progressive increase in the activity of the β-1,3-glucanase and chitinase enzymes required during the hypha elongation process. However, the AN extract progressively reduced FOV sporulation with increasing doses. Furthermore, the cellulolytic capacity of the phytopathogen was significantly reduced in the presence of the algae extract, which was measured by the activity of the enzymes endo-β-1,4-glucanase, exo-β-1,4-glucanase and β-glucosidase. Thus, these facts constitute important information for the management of fusariosis, since the inhibition of sporulation and decreasing degradation capacity of the cellulose by the pathogen, can translate into declined disease in compatible host-pathogen interactions.

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Blanchette, Robert A., André R. Abad, Kory R. Cease, Rex E. Lovrien та Timothy D. Leathers. "Colloidal Gold Cytochemistry of Endo-1,4-β-Glucanase, 1,4-β-D-Glucan Cellobiohydrolase, and Endo-1,4-β-Xylanase: Ultrastructure of Sound and Decayed Birch Wood †". Applied and Environmental Microbiology 55, № 9 (1989): 2293–301. http://dx.doi.org/10.1128/aem.55.9.2293-2301.1989.

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34

Wu, Sheng-Cheng, Jeffrey E. Halley, Christopher Luttig, Linda M. Fernekes, Gerardo Gutiérrez-Sanchez, Alan G. Darvill та Peter Albersheim. "Identification of an endo-β-1,4-d-Xylanase from Magnaporthe grisea by Gene Knockout Analysis, Purification, and Heterologous Expression". Applied and Environmental Microbiology 72, № 2 (лютий 2006): 986–93. http://dx.doi.org/10.1128/aem.72.2.986-993.2006.

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ABSTRACT Magnaporthe grisea, a destructive ascomycetous pathogen of rice, secretes cell wall-degrading enzymes into a culture medium containing purified rice cell walls as the sole carbon source. From M. grisea grown under the culture conditions described here, we have identified an expressed sequenced tag, XYL-6, a gene that is also expressed in M. grisea-infected rice leaves 24 h postinoculation with conidia. This gene encodes a protein about 65% similar to endo-β-1,4-d-glycanases within glycoside hydrolase family GH10. A M. grisea knockout mutant for XYL-6 was created, and it was shown to be as virulent as the parent strain in infecting the rice host. The proteins secreted by the parent strain and by the xyl-6Δ mutant were each fractionated by liquid chromatography, and the collected fractions were assayed for endo-β-1,4-d-glucanase or endo-β-1,4-d-xylanase activities. Two protein-containing peaks with endo-β-1,4-d-xylanase activity secreted by the parent strain are not detectable in the column eluant of the proteins secreted by the mutant. The two endoxylanases (XYL-6α and XYL-6β) from the parent were each purified to homogeneity. N-terminal amino acid sequencing indicated that XYL-6α is a fragment of XYL-6β and that XYL-6β is identical to the deduced protein sequence encoded by the XYL-6 gene. Finally, XYL-6 was introduced into Pichia pastoris for heterologous expression, which resulted in the purification of a fusion protein, XYL-6H, from the Pichia pastoris culture filtrate. XYL-6H is active in cleaving arabinoxylan. These experiments unequivocally established that the XYL-6 gene encodes a secreted endo-β-1,4-d-xylanase.

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Nakatani, Yoshio, Iain L. Lamont та John F. Cutfield. "Discovery and Characterization of a Distinctive Exo-1,3/1,4-β-Glucanase from the Marine Bacterium Pseudoalteromonas sp. Strain BB1". Applied and Environmental Microbiology 76, № 20 (20 серпня 2010): 6760–68. http://dx.doi.org/10.1128/aem.00758-10.

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ABSTRACT Marine bacteria residing on local red, green, and brown seaweeds were screened for exo-1,3-β-glucanase (ExoP) activity. Of the 90 bacterial species isolated from 32 seaweeds, only one, a Pseudoalteromonas sp., was found to display such activity. It was isolated from a Durvillaea sp., a brown kelp known to contain significant amounts of the storage polysaccharide laminarin (1,3-β-d-glucan with some 1,6-β branching). Four chromatographic steps were utilized to purify the enzyme (ExoP). Chymotryptic digestion provided peptide sequences for primer design and subsequent gene cloning. The exoP gene coded for 840 amino acids and was located just 50 bp downstream from a putative lichenase (endo-1,3-1,4-β-glucanase) gene, suggesting possible cotranscription of these genes. Sequence comparisons revealed ExoP to be clustered within a group of bacterial glycosidases with high similarity to a group of glycoside hydrolase (GH3) plant enzymes, of which the barley exo-1,3/1,4-β-glucanase (ExoI) is the best characterized. The major difference between the bacterial and plant proteins is an extra 200- to 220-amino-acid extension at the C terminus of the former. This additional sequence does not correlate with any known functional domain, but ExoP was not active against laminarin when this region was removed. Production of recombinant ExoP allowed substrate specificity studies to be performed. The enzyme was found to possess similar levels of exoglucanase activity against both 1,4-β linkages and 1,3-β linkages, and so ExoP is designated an exo-1,3/1,4-β-exoglucanase, the first such bacterial enzyme to be characterized. This broader specificity could allow the enzyme to assist in digesting both cell wall cellulose and cytoplasmic laminarin.

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Lafond, Mickael, David Navarro, Mireille Haon, Marie Couturier та Jean-Guy Berrin. "Characterization of a Broad-Specificity β-Glucanase Acting on β-(1,3)-, β-(1,4)-, and β-(1,6)-Glucans That Defines a New Glycoside Hydrolase Family". Applied and Environmental Microbiology 78, № 24 (28 вересня 2012): 8540–46. http://dx.doi.org/10.1128/aem.02572-12.

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ABSTRACTHere we report the cloning of thePa_3_10940gene from the coprophilic fungusPodospora anserina, which encodes a C-terminal family 1 carbohydrate binding module (CBM1) linked to a domain of unknown function. The function of the gene was investigated by expression of the full-length protein and a truncated derivative without the CBM1 domain in the yeastPichia pastoris. Using a library of polysaccharides of different origins, we demonstrated that the full-length enzyme displays activity toward a broad range of β-glucan polysaccharides, including laminarin, curdlan, pachyman, lichenan, pustulan, and cellulosic derivatives. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4), and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme performs in an exo-type mode on the nonreducing end of gluco-oligosaccharides. Excision of the CBM1 domain resulted in an inactive enzyme on all substrates tested. To our knowledge, this is the first report of an enzyme that displays bifunctional exo-β-(1,3)/(1,6) and endo-β-(1,4) activities toward beta-glucans and therefore cannot readily be assigned to existing Enzyme Commission groups. The amino acid sequence has high sequence identity to hypothetical proteins within the fungal taxa and thus defines a new family of glycoside hydrolases, the GH131 family.

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Hung, Yu-Lung, Hui-Jye Chen, Jeng-Chen Liu та Yo-Chia Chen. "Catalytic Efficiency Diversification of Duplicate β-1,3-1,4-Glucanases from Neocallimastix patriciarum J11". Applied and Environmental Microbiology 78, № 12 (6 квітня 2012): 4294–300. http://dx.doi.org/10.1128/aem.07473-11.

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ABSTRACTFour types of β-1,3-1,4 glucanase (β-glucanase, EC 3.2.1.73) genes, designatedbglA13,bglA16,bglA51, andbglM2, were found in the cDNA library ofNeocallimastix patriciarumJ11. All were highly homologous with each other and demonstrated a close phylogenetic relationship with and a similar codon bias toStreptococcus equinus. The presence of expansion and several predicted secondary structures in the 3′ untranslated regions (3′UTRs) ofbglA16andbglM2suggest that these two genes were duplicated recently, whereasbglA13andbglA16, which contain very short 3′UTRs, were replicated earlier. These findings indicate that the β-glucanase genes fromN. patriciarumJ11 may have arisen by horizontal transfer from the bacterium and subsequent duplication in the rumen fungus. β-Glucanase genes ofStreptococcus equinus,Ruminococcus albus7, andN. patriciarumJ11 were cloned and expressed byEscherichia coli. The recombinant β-glucanases cloned fromS. equinus,R. albus7, andN. patriciarumJ11 were endo-acting and had similar substrate specificity, but they demonstrated different properties in other tests. The specific activities and catalytic efficiency of the bacterial β-glucanases were also significantly lower than those of the fungal β-glucanases. Our results also revealed that the activities and some characteristics of enzymes were changed during the horizontal gene transfer event. The specific activities of the fungal β-glucanases ranged from 26,529 to 41,209 U/mg of protein when barley-derived β-glucan was used as the substrate. They also demonstrated similar pH and temperature optima, substrate specificity, substrate affinity, and hydrolysis patterns. Nevertheless, BglA16 and BglM2, two recently duplicated β-glucanases, showed much higherkcatvalues than others. These results support the notion that duplicated β-glucanase genes, namely,bglA16andbglM2, increase the reaction efficiency of β-glucanases and suggest that the catalytic efficiency of β-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms inN. patriciarumJ11.

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Fülöp, László, та Tamás Ponyi. "Rapid screening for endo-β-1,4-glucanase and endo-β-1,4-mannanase activities and specific measurement using soluble dye-labelled substrates". Journal of Microbiological Methods 29, № 1 (квітень 1997): 15–21. http://dx.doi.org/10.1016/s0167-7012(97)00984-6.

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39

Ningsih, Dea Aprillia, and Lisa Lisdiana. "Analisis In-silico Struktur Enzim Endo-1,4-B-Glucanase pada Bakteri Fervidobacterium nodosum dan Bacillus subtilis." LenteraBio : Berkala Ilmiah Biologi 11, no. 1 (November 30, 2021): 153–60. http://dx.doi.org/10.26740/lenterabio.v11n1.p153-160.

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Enzim endo 1,4-B-glucanase merupakan enzim yang dapat menghidrolisis selulosa dengan cara memutus ikatan gilosidik-Î²-1,4 dalam selulosa dan turunannya menjadi glukosa. Enzim ini dapat ditemukan pada banyak organisme dengan aktivitas degradasi yang berbeda, misalnya pada bakteri Fervidobacterium nodosum yang bersifat hipertermofilik dan Bacillus subtilis yang bersifat termofilik. Penelitian ini bertujuan untuk mengetahui struktur protein dan similaritas dari kedua enzim endo 1,4-Î²-glucanase berdasarkan urutan sekuen asam amino dan struktur tiga dimensi bakteri F. nodosum dan B. subtilis yang diisolasi dari sumber mata air panas dan fermentasi pakan ternak. Penelitian ini merupakan penelitian deskriptif dengan menggunakan sekuen asam amino kedua enzim yang diperoleh dari situs NCBI (National Center of Biotechnology Information) melalui data mining. Sekuen asam amino yang diperoleh selanjutnya dianalisis similaritasnya melalui penyejajaran sekuen dengan aplikasi Clustal Omega untuk menyejajarkan urutan protein yang berbeda serta untuk memperoleh area lestari. Selanjutnya struktur tiga dimensi kedua enzim diperoleh dari template yang ada pada SWISS MODEL workspace akan dianalisis secara deskriptif. Hasil penelitian ini adalah similaritas enzim endo 1,4-Î²-glucanase pada kedua bakteri sebesar 21,72%. Selain itu ditemukannya empat motif pada struktur tiga dimensi yang diduga mempengaruhi perubahan aktivitas katalitik, stabilitas struktur protein, pembentukan Î±-helix pada kedua struktur protein serta memberikan dampak secara langsung yang berkaitan dengan kemampuan pengikatan selulosa dari masing-masing ikatan domain selulase dan aktivitas enzimatik terhadap selulosa. Perbedaan struktur tiga dimensi enzim endo-1,4-Î²-glucanase pada kedua bakteri diduga mempengaruhi aktivitasnya sehingga diharapkan mampu memberikan kontribusi terhadap penelitian lebih lanjut terkait perbedaan aktivitas degradasi enzim yang diperoleh dari organisme yang berbeda.

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Zhu, Yanman, Yongmei He, Bo Wang, Rihe Peng та Quanhong Yao. "Characterization of a Novel endo-β-1,4-glucanase from the Model Soft Rot Phytopathogen Pectobacterium wasabiae SCC3193". Journal of Pure and Applied Microbiology 12, № 1 (30 березня 2018): 01–12. http://dx.doi.org/10.22207/jpam.12.1.01.

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W.S. Wong, Dominic, Victor J. Chan та Amanda A. McCormack. "Comparative Characterization of a Bifunctional endo-1,4-β-Mannanase/ 1,3-1,4-β-glucanase and its Individual Domains". Protein & Peptide Letters 20, № 5 (1 березня 2013): 517–23. http://dx.doi.org/10.2174/0929866511320050004.

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Sandhu, D. K., та R. Puri. "The developmental patterns of endo-β-1,4-glucanase and β-glucosidase of Chaetomium erraticum". Canadian Journal of Botany 66, № 11 (1 листопада 1988): 2162–66. http://dx.doi.org/10.1139/b88-298.

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The present investigation deals with the production of extracellular and intracellular endoglucanase and β-glucosidase enzymes and the study of their multiple molecular forms in Chaetomium erraticum. When C. erraticum was grown on carboxymethyl cellulose as the sole carbon source, more than 90% of the endoglucanase was extracellular, while most of the β-glucosidase was intracellular. However, the relative distribution of these enzymes varied with the age of the culture. Two forms of each of endoglucanase (EG-I, EG-II) and β-glucosidase (βGlu-I, βGlu-II) were detected after 4 and 6 days of incubation, respectively. Additional intracellular forms of endoglucanase and β-glucosidase i.e., EG-III and βGlu-III, appeared at later stages, when perithecia developed, indicating that EG-III and βGlu-III are related to the development of perithecia. These multiple molecular forms were further differentiated by their response to temperature, pH, ethylenediaminetetraacetic acid, and metal ions.

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Yamanobe, Takashi, та Yasushi Mitsuishi. "Purification of Endo-1,4-/β-glucanase Components from Fungal Strain Y-94". Agricultural and Biological Chemistry 54, № 2 (лютий 1990): 301–7. http://dx.doi.org/10.1080/00021369.1990.10869969.

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Kumar, R., J. S. Dahiya, D. Singh та P. Nigam. "Production of endo-1,4-β-glucanase by a biocontrol fungus Cladorrhinum foecundissimum". Bioresource Technology 75, № 1 (жовтень 2000): 95–97. http://dx.doi.org/10.1016/s0960-8524(00)00037-7.

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Loprete, Darlene M., та Terry W. Hill. "Isolation and characterization of an endo-(1,4)-β-glucanase secreted byAchlya ambisexualis". Mycologia 94, № 6 (листопад 2002): 903–11. http://dx.doi.org/10.1080/15572536.2003.11833148.

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SAMI, AMTUL JAMIL, та M. WAHEED AKHTER. "Multiplicity of the endo-1,4-β-d-glucanase activity in Cellulomonas flavigena". Biochemical Society Transactions 17, № 3 (1 червня 1989): 580–81. http://dx.doi.org/10.1042/bst0170580.

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Stutzenberger, Fred, та Davis Lupo. "pH-dependent thermal activation of endo-1,4-β-glucanase in Thermomonospora curvata". Enzyme and Microbial Technology 8, № 4 (квітень 1986): 205–8. http://dx.doi.org/10.1016/0141-0229(86)90088-8.

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