Готові списки джерел за темами / Endo-(1,4)-β-glucanase

Добірка наукової літератури з теми "Endo-(1,4)-β-glucanase"

Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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

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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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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Анотація:
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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Анотація:
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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Анотація:
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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Більше джерел

Дисертації з теми "Endo-(1,4)-β-glucanase"

1

Woolley, Lindsey C. "The role of endo-#beta#-1,4-glucanase in strawberry fruit development." Thesis, Open University, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.340705.

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2

Akiba, Shunichi. "Studies on Protease-Resistant Endo-β-1, 4-glucanase from Aspergillus niger". Kyoto University, 1999. http://hdl.handle.net/2433/181918.

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3

Robert, Stéphanie. "Etude de la protéine KORRIGAN, une endo-β-1,4-glucanase impliquée dans la synthèse de cellulose chez Arabidopsis thaliana et Gossypium hirsutum". Paris 11, 2005. http://www.theses.fr/2005PA112007.

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Анотація:
Afin de mieux comprendre les mécanismes moléculaires régissant la synthèse de cellulose chez les végétaux, je me suis intéressée à la protéine KORRIGAN1, une endo--1,4-glucanase. La première partie de ma thèse a été consacrée à l’étude de KOR1 au sein d’un complexe multiprotéique membranaire chez Arabidopsis et le cotonnier. La mise en évidence d’une différence de taille de ce complexe en fonction du niveau de synthèse de la cellulose laisse supposer un lien étroit entre la formation de ce complexe et la fonction de KOR. Différents partenaires potentiels de KOR1 au sein de ce complexe ont été identifiés, révélant de potentielles interactions entre KOR1 et le cytosquelette. Le rôle de KOR1 a aussi été abordé, et notamment son implication dans le recyclage d’amorces lipidiques. Cette fonction hypothétique appuyée par des résultats obtenus chez le cotonnier, n’a pas été confortée par études réalisées chez Arabidopsis. Je me suis enfin intéressée à la localisation subcellulaire de KOR1. KOR1 est localisée dans des compartiments intracellulaires, distincts de l’appareil de Golgi, et qui colocalisent partiellement avec les endosomes précoces. Ces compartiments sont mobiles et cette motilité dépend d’un réseau de microtubules intact mettant à nouveau en évidence un lien entre KOR1 et les éléments du cytosquelette. Lorsque la synthèse de cellulose est inhibée par de l’isoxabène, les compartiments contenant KOR1 sont plus près de la membrane plasmique et distincts des endosomes précoces. Ceci suggère donc que la synthèse de cellulose est fortement contrôlée, notamment à travers la régulation de la localisation et des interactions des protéines enzymatiques y participant
In order to better understand the molecular mechanisms that govern cellulose synthesis, KORRIGAN1, an endo--1,4-glucanase involved in this process, has been studied. In the first part of my thesis, KOR1 was shown to be present in high molecular weight complexes in Arabidopsis thaliana and cotton fibers. The weight of this complex changes in function of the level of cellulose synthesis, demonstrating that cellulose synthesis and KOR1 function are linked. Different putative protein partners have been identified which suggest a close interaction between KOR1 and the cytoskeleton. It has been suggested that KOR1 may recycle sitosterol primers involved in the initiation of celullose synthesis in cotton fibers. In the second part of my thesis, I tested this hypothesis and the results obtained suggest that this hypothetic function is not real. Finally, I focussed on the subcellular localization of KOR1. Using a variety of methods, we showed that KOR1 was present in intracellular compartments, distinct from the Golgi apparatus and showing some colocalization with endosomal compartments. These compartments were very motile in a microtubules integrity dependent manner, linking KOR1 to the cytoskeleton again. When cellulose synthesis was inhibited, the KOR1 compartments were closer to the plasma membrane and distinct from the endosomal compartments. These results suggest that cellulose synthesis is highly regulated through the control of the localisation and interaction of the enzymes involved in this process
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4

Phan, Minh Thi Tuyet, Viet Quoc Nguyen, Hy Gia Le, Thoa Kim Nguyen та Man Dinh Tran. "Molecular cloning gene and nucleotide sequence of the gene encoding an endo-1,4-β-glucanase from Bacillus sp VLSH08 strain applying to biomass hydrolysis". Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-99522.

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Bacillus sp VLSH08 screened from sea wetland in Nam Dinh province produces an extracellular endo-1,4-beta-glucanase. According to the results of the classified Kit API 50/CHB as well as sequence of 1500 bp fragment coding for 16S rRNA gene of the Bacillus sp VLSH 08 strain showed that the taxonomical characteristics between the strain VLSH 08 and Bacillus amyloliquefaciene JN999857 are similar of 98%. Culture supernatant of this strain showed optimal cellulase activity at pH 5.8 and 60 Celsius degree and that was enhanced 2.03 times in the presence of 5 mM Co2+. Moreover, the gene encoding endo-1,4-beta-glucanase from this strain was cloned in Escherichia coli using pCR2.1 vector. The entire gene for the enzyme contained a 1500-bp single open reading frame encoding 500 amino acids, including a 29-amino acid signal peptide. The amino acid sequence of this enzyme is very close to that of an EG of Bacillus subtilis (EU022560.1) and an EG of Bacillus amyloliquefaciene (EU022559.1) which all belong to the cellulase family E2. A cocktail of enzyme containing this endo-1,4-beta-glucanase used for biomass hydrolysis indicated that the cellulose conversion attained to 72.76% cellulose after 48 hours
Chủng vi khuẩn Bacillus sp VLSH08 được tuyển chọn từ tập hợp chủng vi khuẩn phân lập ở vùng ngập mặn tỉnh Nam Định có khả năng sinh tổng hợp enzyme endo-1,4-beta-glucanase ngoại bào. Kết quả phân loại chủng vi khuẩn Bacillus sp VLSH08 bằng Kit hóa sinh API 50/CHB cũng như trình tự gen mã hóa 16S rRNA cho thấy độ tương đồng của chủng Bacillus sp VLSH08 và chủng Bacillus amyloliquefaciene JN999857 đạt 98%. Dịch lên men của chủng được sử dụng làm nguồn enzyme thô để nghiên cứu hoạt độ tối ưu của enzyme ở pH 5,8 và nhiệt đô 60oC. Hoạt tính enzyme tăng 2,03 lần khi có mặt 5 mM ion Co2+. Đồng thời, gen mã hóa cho enzyme endo-1,4-betaglucanase cũng được tách dòng trong tế bào Escherichia coli sử dụng vector pCR 2.1. Gen mã hóa cho enzyme này có chiều dài 1500 bp, mã hóa cho 500 axit amin, bao gồm 29 axit amin của chuỗi peptid tín hiệu. So sánh cho thấy trình tự gen endo-1,4-beta-glucanase của chủng Bacillus sp VLSH08 có độ tương đồng cao với enzyme này của chủng Bacillus subtilis (EU022560.1) và của chủng Bacillus amyloliquefaciene (EU022559.1). Tất cả các enzyme nhóm này đều thuộc họ cellulase E2. Enzyme của chủng này cũng đã được phối trộn với các enzyme khác tạo thành cocktail để thủy phân sinh khối cho kết quả cellulose bị thủy phân 72,76% sau 48 giờ
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5

Louw, Maureen Elizabeth. "Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon". Doctoral thesis, University of Cape Town, 1994. http://hdl.handle.net/11427/21696.

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Bibliography: pages 127-144.
Bacillus brevis Alk 36 was isolated from soil during a screening programme for the selection of extracellular enzyme producing strains. A gene coding for an endo(1,3- 1,4 )-.8-glucanase (or lichenase) was cloned from B. brevis Alk 36 and expressed in Escherichia coli. The nucleotide sequence of this gene was determined and found to encode a protein of 252 amino acid residues. The amino acid sequence of the B. brevis lichenase gene showed only a 50% similarity to previously published data for Bacillus endo-(1,3-1,4)-β-glucanases. The enzyme exhibited some unique properties. The optimum temperature and pH for enzyme activity were 65-70°C and 8-10, respectively. When held at 75°C for 1 h, 75% residual activity was measured. The molecular mass was estimated to be 29 kDa and the enzyme was found to be resistant to sodium dodecyl sulphate (SDS). B. brevis Alk 36 was evaluated as a potential host strain for the efficient production and secretion of foreign proteins and was found to grow optimally between pH 8.0 and pH 9.5 and between 42°C and 52°C. B. brevis was successfully transformed using vector DNA and was found to produce relatively low levels of protease. In addition, it was evaluated as a possible protein hyper-secreting strain. However, using PCR technology, the highly conserved cell wall protein genes could not be positively identified in B. brevis Alk 36.
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6

Tarrés, Farrés Joaquim Agustí. "Endo-β-1,4-glucanasa para la fabricación de micro/nanocelulosa: propiedades y aplicaciones". Doctoral thesis, Universitat de Girona, 2017. http://hdl.handle.net/10803/456211.

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In the recent years, significant interest on the production, characterization and application of cellulose nanofibers has brought out among scientific and technic authorities. This special attention mainly comes from their biodegradability, renewability and versatility, making them able to be used for several applications and fields. This topic outbreak took place about ten years ago, fact that is confirmed by the exponential increase on scientific publications and patents since then. In a nutshell, the present thesis aims to demonstrate that enzymatically hydrolyzed cellulose nanofibers can be successfully produced and used in several sectors. Their versatility, availability, low cost and low environmental impact justify the ongoing research in this field
En els darrers anys, entre la comunitat científica i tecnològica s’ha despertat un gran interès en la producció, caracterització i utilització de nanofibres de cel·lulosa. Aquesta especial atenció es deu, principalment, al seu caràcter biodegradable, el seu origen renovable i la versatilitat que presenten, fent-les aptes per ser utilitzades en multitud d’aplicacions. L’esclat d’aquesta temàtica de recerca va tenir lloc aproximadament deu anys enrere, doncs només cal observar el creixement exponencial de publicacions científiques i patents des d’aleshores. De manera general, la present tesi pretén demostrar que les nanofibres de cel·lulosa obtingudes mitjançant un pretractament d’hidròlisi enzimàtica poden ser produïdes de forma efectiva, de manera que pugin ser aplicades en una gran varietat de camps científics i tecnològics. La seva gran versatilitat, disponibilitat, baix cost i baix impacte mediambiental, justifiquen que en el futur es continuï amb la seva investigació sobre noves aplicacions
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Stronach, Morag Shona. "The molecular cell biology of a xyloglucan specific endo 1,4 #beta#-D-glucanase from Tropaeolum majus L. cotyledons." Thesis, University of Stirling, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294012.

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Silva, Caio de Oliveira Gorgulho. "Emericella nidulans e bagaço de cana-de-açucar : ferramentas para produção de endo-β-1,4-xilanase". reponame:Repositório Institucional da UnB, 2014. http://repositorio.unb.br/handle/10482/15669.

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Dissertação (mestrado)—Universidade de Brasília, Instituto de Ciências Biológicas, Programa de Pós-Graduação em Biologia Molecular, 2014.
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O bagaço de cana-de-açúcar é um importante resíduo agroindustrial brasileiro que apresenta grande potencial para ser utilizado como fonte de carbono para produção de holocelulases de interesse industrial por microrganismos. As xilanases, objeto de estudo deste trabalho, são enzimas que apresentam uma série de aplicações biotecnológicas que incluem a produção de etanol de segunda geração, o branqueamento de papel, a produção de sucos e pães e o uso como aditivo em rações animais. O objetivo desta pesquisa foi purificar e caracterizar uma xilanase produzida pelo fungo Emericella nidulans quando cultivado em bagaço de cana, visando o aproveitamento deste resíduo e a avaliação do potencial biotecnológico da enzima. O fungo foi capaz de secretar xilanases a partir do primeiro dia de cultivo sob fermentação submersa utilizando o bagaço. Uma xilanase de 22 kDa foi purificada a partir do extrato bruto obtido no cultivo através de ultrafiltração, precipitação com sulfato de amônio e cromatografias de filtração em gel e troca aniônica. A enzima apresentou alta homologia com endo-β-1,4-xilanase A (XynA) de E. nidulans e desta forma foi chamada. A enzima XynA apresentou maior atividade a 55°C e na faixa de pH 3,0 – 6,5. A enzima se mostrou pouco termoestável, com meiasvidas de 40, 10 e 7 minutos a 28, 50 e 55°C, respectivamente. XynA foi mais ativa sobre a porção solúvel da xilana, com valores de KM e Vmáx 3,39 mg/mL e 0,502 UI/mL, respectivamente. A hidrólise da xilana por XynA gerou xilooligossacarídeos, indicando ação tipo endo. Diferentes compostos fenólicos comumente liberados durante o pré-tratamento de biomassa lignocelulósica causaram efeitos variados sobre XynA. Os ácidos tânico e cinâmico inibiram a enzima, enquanto o ácido 4-hidroxi-benzóico aumentou sua atividade e os ácidos ferúlico, p-cumárico e vanilina não mostraram efeito. O etanol aumentou a atividade, estabilidade e Vmáx da enzima, indicando potencial para aplicação em processos de sacarificação e fermentação simultâneas de biomassa. O ultrafiltrado (uma fração semipurificada de xilanases) foi capaz de hidrolisar polpas de celulose em diferentes etapas do processo Kraft, resultando na liberação de açúcares redutores, cromóforos, pentoses e produtos de hidrólise de xilana sem concomitante liberação de glicose. O extrato bruto se mostrou capaz de degradar bagaço de cana-de-açúcar não-tratado ou sumetido a explosão a vapor, liberando açúcares redutores e produtos de hidrólise de xilana. ______________________________________________________________________________ ABSTRACT
Sugarcane bagasse is a major lignocellulosic agroindustrial residue in Brazil with great potencial for utilization as carbon source for production of industrial holocellulases by microrganisms. Xylanases present several biotechnological applications such as in ethanol production, paper bleaching, juice and bread production and utilization as feed additive. The goal of this reseach was to purify and characterize one xylanase produced by the fungus Emericella nidulans when grown on sugarcane bagasse, aiming the use of this residue and the investigation of biotechnological potencials of the enzyme. E. nidulans secreted xylanases from the first day of growth on liquid media containing bagasse as sole carbon source. One 22 kDa xylanase was purified from crude extract through ultrafiltration, ammonium sulphate precipitation, gelfiltration and anion-exchange chromatographies. The enzyme showed significant homology with endo-β-1,4-xylanase A (XynA) from E. nidulans, and was named that way. XynA was most active at 55°C and pH 3,0 – 6,5. Considering its thermostability, XynA presented half-lives of 40, 10 and 7 minutes at 28, 50 and 55°C, respectively. The enzyme was more active on the soluble portion of xylan, with Km and Vmax values 3,39 mg.mL¯ ¹ and 0,502 UI.mL¯ ¹, respectively. Xylan hydrolysis by XynA produced xylooligossacharides, indicating endo-type action. Phenolic compounds released during pre-treatment of lignocellulosic biomass caused different effects on XynA. Tannic and cinnamic acids inhibited XynA, while 4-hidroxibenzoic acid enhanced its activity and ferulic and p-coumaric acids and vanillin caused no effect. Ethanol increased XynA activity, thermostability and Vmax, suggesting potencial for aplication in simultaneous sacharification and fermentation processes. Ultrafiltrate sample (partialy purified xylanases) was able to hydrolyse celullose pulps obtained from different stages of Kraft process, resulting in release of reducing sugars, chromophores, pentoses and xylans degradation products with apparent no release of glucose. E. nidulans crude extract was able to hydrolyse untreated or steam-explosion pretreated sugarcane bagasses, releasing reducing sugars and xylans degradation products.
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Miotto, Lis Schwartz. "Estudos moleculares, estruturais e funcionais da Cel12A de Gloeophyllum trabeum, uma endo-1,4-β-glucanase da família 12 de hidrolases de glicosídeos." Universidade Federal de São Carlos, 2014. https://repositorio.ufscar.br/handle/ufscar/272.

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Universidade Federal de Minas Gerais
The production of second-generation ethanol by enzymatic hydrolysis of biomass is considered a viable and promising alternative to face the global energy crisis and to decrease our dependence on fossil fuels. Therefore, it is necessary to degrade the constituent molecules of the plant cell wall such as lignin, cellulose and hemicellulose to fermentable sugars. However, the use of enzymes for this purpose is still expensive, leading to the increase on studies seeking to make them more feasible economically and technically. The present study aimed the molecular, structural and functional characterization of the endoglucanase Cel12A from the fungus Gloeophyllum trabeum by different techniques. Biochemical data revealed the substrate specificity for the enzyme and showed that β-glucan is the best substrate for its activity (239.2 ± 9.1 U mg-1). Optimal conditions for activity were pH 4.5 and temperature of 50 oC. Thermal stability assay indicated a half-life of 84.6 ± 3.6 hours at 50 oC. The kinetic parameters Km (3.2 ± 0.5 mg mL-1) and Vmax (0,40 ± 0,02 μmol min-1) were determined using β-glucan as substrate. Analysis of scanning electron microscopy of oat spelts and filter paper samples submitted to the hydrolysis by GtCel12A evidenced the degradation effects of these substrates compared to control samples. Moreover, the low-resolution envelope and the crystallographic structure for GtCel12A were determined. The structure revealed a β-sandwich fold with two β-sheets (A and B) and three α-helices, while sheet A showed five strands and sheet B nine strands. The comparative analysis of the amino acid sequence and homologous structures prompted us to identify the catalytic residues, Glu142 and Glu227 in the active site of the enzyme. These results are important for understanding and elucidating the enzyme molecular mechanism of action and other glycoside hydrolase family 12 endoglucanases.
A produção de etanol de segunda geração, a partir da hidrólise enzimática da biomassa vegetal é considerada uma alternativa viável e promissora para enfrentarmos a crise energética mundial e diminuirmos a dependência das fontes fósseis de energia. Para isso, é necessário que ocorra a degradação das moléculas constituintes da parede celular como a lignina, a celulose e a hemicelulose a açúcares fermentescíveis. No entanto, a utilização de enzimas para esse fim ainda apresenta um custo elevado, o que tem desencadeado, cada vez mais, estudos que busquem torná-las mais viáveis econômica e tecnicamente. O presente estudo visou à caracterização molecular, estrutural e funcional da endoglucanase Cel12A do fungo Gloeophyllum trabeum por diferentes técnicas. Os dados bioquímicos revelaram a especificidade por substratos da enzima, sendo que o melhor substrato para a atividade foi o β-glucano (239,2 ± 9,1 U mg-1). As condições ótimas para a atividade foram pH 4,5 e temperatura de 50 oC. Os ensaios de estabilidade térmica indicaram uma meia-vida de 84,6 ± 3,6 horas a 50 oC. Os parâmetros cinéticos Km (3,2 ± 0,5 mg mL-1)) e Vmax (0,40 ± 0,02 μmol min-1) foram determinados utilizando-se β-glucano como substrato. Análises de microscopia eletrônica de varredura de amostras de papel de filtro e aveia submetidos à hidrólise pela GtCel12A evidenciaram os efeitos de degradação dos substratos em relação às amostras controle. Adicionalmente, o envelope de baixa resolução e a estrutura cristalográfica da GtCel12A foram obtidos. O modelo de alta resolução revelou um enovelamento do tipo sanduíche β, com duas folhas β (A e B) e três hélices α, sendo que a folha A apresentou cinco fitas e a B, nove fitas. Por meio de análises comparativas da sequência de aminoácidos e de estruturas homólogas identificamos os resíduos catalíticos Glu142 e Glu227 no sítio ativo da enzima. Tais resultados são importantes para a elucidação e compreensão do mecanismo molecular de atuação dessa enzima e de outras endoglucanases da família GH12.
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Menu-Bouaouiche, Laurence. "Relations structure-fonction et propriétés de surface de protéines PR5 "thaumatin-like" de fruits comestibles." Toulouse 3, 2003. http://www.theses.fr/2003TOU30171.

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Les protéines PR5 ou thaumatin-like (TLP) forment une famille structurale et phylogénique très homogène, mais elles possèdent in vitro des propriétés disparates : antifongiques, antigel, liaison et/ou hydrolyse de glucane. Certaines d'entre elles sont induites par des stress biotiques ou abiotiques et semblent intervenir dans la protection plus ou moins efficace des plantes vis à vis de pathogènes fongiques. D'autre part, certains fruits accumulent des protéines similaires au cours de leur maturation, dont celles de cerise et de pomme, allergéniques. Une meilleure connaissance des propriétés fonctionnelles et structurales des TLP spécifiques de fruits devrait permettre d'élaborer de nouveaux diagnostics d'allergènes et d'orienter, par rapport aux éventuels risques d'allergie, l'amélioration de la résistance naturelle des plantes. Afin de définir les relations structure-fonction de ces protéines, nous avons, tout d'abord, réalisé l'analyse de la phylogénie, de la structure et des propriétés électrostatiques et hydrophobes de surface de différents membres de la famille, par des techniques d'analyse de séquence et de modélisation moléculaire. .
PR-5 or Thaumatin-like proteins (TLP) are structurally and phylogenetically related but their activities in vitro are very diverse: antifungal, antifreeze, glucan affinity and/or hydrolysis. Some of them are induced by biotic or abiotic stresses and could be involved in plant's defense against pathogenic fungi. In contrast, some fruits accumulate similar proteins during their maturation, like these of cherry or apple that are allergenic A better understanding of functional and structural properties of fruit specific's PR-5 proteins could allow new allergy diagnostics elaboration and new orientations' definition, beware of allergy risks, for natural plant defense amelioration. For the definition of TLP structure-function relationships, we have, first, analyzed different members of this family, for their phylogeny, their structure and their surface electrostatics and hydrophobic properties, by sequence analysis and molecular modeling methodologies. Thereafter, cherry, apple and banana's TLP and Thaumatin were compared for their enzymatic and antifungal activities. .
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Частини книг з теми "Endo-(1,4)-β-glucanase"

1

Brummell, David A., Coralie C. Lashbrook, and Alan B. Bennett. "Plant Endo-1,4-β-D-glucanases." In ACS Symposium Series, 100–129. Washington, DC: American Chemical Society, 1994. http://dx.doi.org/10.1021/bk-1994-0566.ch006.

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Rose, J. K. C., C. Catala, D. A. Brummell, C. C. Lashbrook, C. Gonzalez-Bosch, and A. B. Bennett. "The Tomato Endo-β-1,4-Glucanase Gene Family: Regulation by Both Ethylene and Auxin." In Biology and Biotechnology of the Plant Hormone Ethylene, 197–205. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5546-5_26.

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Lashbrook, Coralie C., and Alan B. Bennett. "Functional Analysis of Cx-cellulase (Endo-β-1,4-Glucanase) Gene Expression in Transgenic Tomato Fruit." In Cellular and Molecular Aspects of the Plant Hormone Ethylene, 123–28. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-017-1003-9_25.

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Annamalai, Neelamegam, Mayavan Veeramuthu Rajeswari, and Thangavel Balasubramanian. "Endo-1,4-β-glucanases: Role, Applications and Recent Developments." In Biofuel and Biorefinery Technologies, 37–45. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43679-1_3.

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Rodrigues, Alexandre Gomes. "Endo-β-1,4-xylanase: An Overview of Recent Developments." In Biofuel and Biorefinery Technologies, 125–49. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43679-1_6.

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6

Trainotti, L., C. A. Tomasin, and G. Casadoro. "Characterization of caEG2, a Pepper Endo-β-1,4-Glucanase Gene Involved in the Abscission of Leaves and Flowers." In Biology and Biotechnology of the Plant Hormone Ethylene II, 269–70. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4453-7_48.

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Shani, Ziv, Mara Dekel, Galit Tsabary, Christian Sig Jensen, Tzvi Tzfira, Raphael Goren, Arie Altman, and Oded Shoseyov. "Expression of Arabidopsis Thaliana Endo-1,4-ß-Glucanase (cel1) in Transgenic Poplar Plants." In Plant Biotechnology and In Vitro Biology in the 21st Century, 209–12. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4661-6_49.

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8

Spezio, Mike, P. Andrew Karplus, Diana Irwin, and David B. Wilson. "Structure—Function Studies of Endo-l,4-β-D-glucanase E2 fromThermomonospora fusca." In ACS Symposium Series, 66–74. Washington, DC: American Chemical Society, 1994. http://dx.doi.org/10.1021/bk-1994-0566.ch003.

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9

Trainotti, L., L. Ferrarese, and G. Casadoro. "Different Endo-β-1,4-Glucanases are Expressed During Abscission and Fruit Ripening in Pepper and Peach Plants." In Biology and Biotechnology of the Plant Hormone Ethylene, 191–96. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5546-5_25.

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McCleary, Barry V., Vincent McKie, and Anna Draga. "Measurement of endo-1,4-β-Glucanase." In Cellulases, 1–17. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-415931-0.00001-x.

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Тези доповідей конференцій з теми "Endo-(1,4)-β-glucanase"

1

AZEVEDO, B., R. A. SILVA, S. S. OLIVEIRA, R. P. VELOSO, S. B. F. SANTOS та L. S. C. OLIVEIRA. "PRODUÇÃO DE ENDO-Β-1,4-GLUCANASE UTILIZANDO SORGO SACARINO IPA P15". У XXII Congresso Brasileiro de Engenharia Química. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/cobeq2018-pt.0606.

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Ribeiro de Assis, Samila, Cristian Lourenço, Camila Telles de Bessa, LUCAS VINÍCIUS TRINDADE, Hamilton Cabral та Gustavo Orlando Bonilla Rodriguez. "Caracterização da endo-1,4-β-D-xilanase do extrato bruto produzido pelo fungo mesofílico Penicillium corylophilum em cultivo submerso". У Simpósio Nacional de Bioprocessos e Simpósio de Hidrólise Enzimática de Biomassa. Campinas - SP, Brazil: Galoá, 2015. http://dx.doi.org/10.17648/sinaferm-2015-33864.

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GAUTÉRIO, G. V., L. C. S. CORRÊA Jr, T. B. MACHADO, M. V. C. V. MATTOS, A. V. L. SANZO та S. J. KALIL. "EFEITO DO PRÉ-TRATAMENTO ALCALINO DA CASCA DE AVEIA PARA PRODUÇÃO DE ENDO-β-1,4-XILANASE POR Aureobasidium pullulans CCT 1261". У XXII Congresso Brasileiro de Engenharia Química. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/cobeq2018-pt.0552.

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GAUTÉRIO, G. V., L. G. G. SILVA, T. HÜBNER, M. C. VIEIRA, A. V. L. SANZO та S. J. KALIL. "PRODUÇÃO DE ENDO-β-1,4-XILANASE POR Aureobasidium pullulans CCT 1261 UTILIZANDO SUBPRODUTOS DO ARROZ COM E SEM PRÉ-TRATAMENTO ALCALINO". У XXII Congresso Brasileiro de Engenharia Química. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/cobeq2018-pt.0878.

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