Academic literature on the topic 'Fungal amylase'
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Journal articles on the topic "Fungal amylase"
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Khushk, Imrana. "Environmental Friendly Production of Amylase from Aspergillus niger EFRL-FC-024 Using Corn Waste as Carbon Source." Pakistan Journal of Analytical & Environmental Chemistry 22, no. 1 (June 23, 2021): 165–71. http://dx.doi.org/10.21743/pjaec/2021.06.17.
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Amylase is an indispensable and industrially important enzyme that hydrolyzes carbohydrates particularly starch into simple sugars. Amylase enzymes have been isolated from various sources such as microbes, animals and plants. However, microorganisms are highly preferred as compared to plants and animal sources. Amylases of fungal origin are highly stable compared to amylases produced by bacterial species. The aim of this study was to investigate the production of extracellular amylase enzyme from Aspergillus niger EFRL-FC-024 using sugarcane bagasse and corn waste as an energy source under submerge fermentation conditions. Primarily, the fungal strain was grown for 6 days using sugarcane bagasse and corn waste, respectively. Mainly, the growth of a microorganism was also evaluated using different pH, temperature and incubation periods. The results revealed maximum amylase production of 1.64 U/mL when A. niger was cultured for 96 h using corn waste. Moreover, addition of different nitrogen sources showed the highest amylase production when peptone was supplemented as a nitrogen source. Finally, the effect of pH indicated maximal concentration of amylase enzyme at pH 6.0. The present study will highly be beneficial to explore the role of fungal strain A. niger in amylase production at Industrial levels.
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Singh, Shalini, Sanamdeep Singh, Vrinda Bali, Lovleen Sharma, and Jyoti Mangla. "Production of Fungal Amylases Using Cheap, Readily Available Agriresidues, for Potential Application in Textile Industry." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/215748.
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The study aimed at isolation and screening of fungal amylase producer, optimization of solid state fermentation conditions for maximum amylase production by the best amylase producer, and characterization of the crude amylases, so produced.Aspergillus fumigatusNTCC1222 showed the highest amylase activity (164.1 U/mL) in secondary screening under SSF conditions and was selected for further studies. The test strain showed maximum amylase production (341.7 U/mL) and supernatant protein concentration (9.7 mg/mL) for incubation period (6 days), temperature (35°C), initial pH (6.0), nutrient salt solution as moistening agent, and beef extract as nitrogen source. Pomegranate peel produced maximum amylase activity, but wheat bran (only slightly lesser amylase activity as compared to that of pomegranate peel) was chosen for further studies, keeping in mind the seasonal availability of pomegranate peel. TLC confirmed the amylase produced to beα-type and 60 kDa was the molecular weight of the partially purified amylase. The enzyme showed maximum enzyme activity at pH 6.0, temperature of 55°C, and incubation time of 60 minutes. UV (616.0 U/mL) and chemical (814.2 U/mL) mutation enhanced amylase activity as compared to wild test strain. The study indicates thatAspergillus fumigatusNTCC1222 can be an important source of amylase and the crude enzyme, hence obtained, can be cost effectively applied in multiple sections of textile wet processing.
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Okunwaye, T., P. O. Uadia, B. O. Okogbenin, E. A. Okogbenin, D. C. Onyia, and J. U. Obibuzor. "Amylase-Producing Fungi and Bacteria Associated with Some Food Processing Wastes." Nigerian Journal of Biotechnology 38, no. 1 (July 27, 2021): 74–82. http://dx.doi.org/10.4314/njb.v38i1.9.
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Amylases are enzymes that catalyze the hydrolysis of glycosidic bonds present in starch to release simple sugars. They are one of the most important enzymes in numerous commercial processes. In this investigation, fungal and bacterial strains from the following agro-industrial wastes were isolated and screened for amylolytic ability: soil from oil palm plantation, shea seed, date fruit, coconut meat, cassava effluent, cassava peel, cassava tubers, yam and potato tubers, starch medium, parboiled water from noodles and rice. The results revealed the presence of Geotrichum, Aspergillus, Penicillium, Trichoderma, Rhizopus and Fusarium spp. Five major genera of bacterial species namely Corynebacterium, Pseudomonas, Lactobacillus, Micrococcus and Bacillus were isolated and screened for amylase activity. Cassava soil had the highest heterotrophic bacterial count of 5.7 x105cfu/g and coconut meat waste had the lowest heterotrophic bacterial count of 1.3 x105cfu/g. All isolated microorganisms had the amylolytic ability. The fungal isolates had higher amylase activity when compared with the bacterial isolates. This investigation reveals organisms with high amylase activity.
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Roth, Christian, Olga V. Moroz, Johan P. Turkenburg, Elena Blagova, Jitka Waterman, Antonio Ariza, Li Ming, et al. "Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance." International Journal of Molecular Sciences 20, no. 19 (October 3, 2019): 4902. http://dx.doi.org/10.3390/ijms20194902.
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Amylases are probably the best studied glycoside hydrolases and have a huge biotechnological value for industrial processes on starch. Multiple amylases from fungi and microbes are currently in use. Whereas bacterial amylases are well suited for many industrial processes due to their high stability, fungal amylases are recognized as safe and are preferred in the food industry, although they lack the pH tolerance and stability of their bacterial counterparts. Here, we describe three amylases, two of which have a broad pH spectrum extending to pH 8 and higher stability well suited for a broad set of industrial applications. These enzymes have the characteristic GH13 α-amylase fold with a central (β/α)8-domain, an insertion domain with the canonical calcium binding site and a C-terminal β-sandwich domain. The active site was identified based on the binding of the inhibitor acarbose in form of a transglycosylation product, in the amylases from Thamnidium elegans and Cordyceps farinosa. The three amylases have shortened loops flanking the nonreducing end of the substrate binding cleft, creating a more open crevice. Moreover, a potential novel binding site in the C-terminal domain of the Cordyceps enzyme was identified, which might be part of a starch interaction site. In addition, Cordyceps farinosa amylase presented a successful example of using the microseed matrix screening technique to significantly speed-up crystallization.
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Fakhoury, A. M., and C. P. Woloshuk. "Inhibition of Growth of Aspergillus flavus and Fungal α-Amylases by a Lectin-Like Protein from Lablab purpureus." Molecular Plant-Microbe Interactions® 14, no. 8 (August 2001): 955–61. http://dx.doi.org/10.1094/mpmi.2001.14.8.955.
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Aspergillus flavus is a fungal pathogen of maize causing an important ear rot disease when plants are exposed to drought and heat stress. Associated with the disease is the production of aflatoxins, which are a series of structurally related mycotoxins known to be carcinogenic. Previous research has suggested that the α-amylase of A. flavus promotes aflatoxin production in the endosperm of infected maize kernels. We report here the isolation and characterization of a 36-kDa α-amylase inhibitor from Lablab purpureus (AILP). AILP inhibited the α-amylases from several fungi but had little effect on those from animal and plant sources. The protein inhibited conidial germination and hyphal growth of A. flavus. The amino acid sequence indicated that AILP is similar to lectin members of a lectin-arcelin-α-amylase inhibitor family described in common bean and shown to be a component of plant resistance to insect pests. AILP also agglutinated papain-treated red blood cells from human and rabbit. These data indicate that AILP represents a novel variant in the lectin-arcelin-α-amylase inhibitor family of proteins having lectin-like and α-amylase inhibitory activity.
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Chen, Z. Y., R. L. Brown, J. S. Russin, A. R. Lax, and T. E. Cleveland. "A Corn Trypsin Inhibitor with Antifungal Activity Inhibits Aspergillus flavus α-Amylase." Phytopathology® 89, no. 10 (October 1999): 902–7. http://dx.doi.org/10.1094/phyto.1999.89.10.902.
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In this study, we found that the inhibition of fungal growth in potato dextrose broth (PDB) medium by the 14-kDa corn trypsin inhibitor (TI) protein, previously found to be associated with host resistance to aflatoxin production and active against various fungi, was relieved when exogenous α-amylase was added along with TI. No inhibitory effect of TI on fungal growth was observed when Aspergillus flavus was grown on a medium containing either 5% glucose or 1% gelatin as a carbon source. Further investigation found that TI not only inhibited fungal production of extracellular α-amylase when A. flavus was grown in PDB medium containing TI at 100 μg ml-1 but also reduced the enzymatic activity of A. flavus α-amylase by 27%. At a higher concentration, however, TI stimulated the production of α-amylase. The effect of TI on the production of amyloglucosidase, another enzyme involved in starch metabolism by the fungus, was quite different. It stimulated the production of this enzyme during the first 10 h at all concentrations studied. These studies suggest that the resistance of certain corn genotypes to A. flavus infection may be partially due to the ability of TI to reduce the production of extracellular fungal α-amylase and its activity, thereby limiting the availability of simple sugars for fungal growth. However, further investigation of the relationship between TI levels and fungal α-amylase expression in vivo is needed.
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Słomińska, Lucyna, Roman Zielonka, and Leszek Jarosławski. "The unconventional single stage hydrolysis of potato starch." Polish Journal of Chemical Technology 15, no. 3 (September 1, 2013): 7–14. http://dx.doi.org/10.2478/pjct-2013-0037.
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Abstract Enzymatic depolymerisation of starch to glucose or maltose is carried out by starch- degrading amylases during a two-stage hydrolysis: liquefaction using bacterial α-amylase followed by saccharification with glucogenic (fungal amylase) or maltogenic (fungal or bacterial) amylases. As a rule, these enzymes are applied separately, following the recommendations concerning their action provided by the enzyme manufacturers. The study presents our attempts to determine the reaction conditions for a simultaneous action of liquefying and saccharifying enzymes on pre-treated potato starch. Hydrolysis was run by Liquozyme Supra, Maltogenase 4000L and San Super 360L enzymes (Novozymes) at different temperatures. During the single-stage method of starch hydrolysate production the most desirable results was obtained for the maltose hydrolysate at 80°C (51.6 DE) and for the glucose hydrolysate at 60°C (96 DE). The analyses indicate that the application of a single-stage hydrolysis of starch to maltose or glucose makes it possible to obtain a degree of starch saccharification comparable with that obtained in the traditional two-stage hydrolysis.
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Sariozlu, N. Yilmaz, and R. Demirel. "Screening of fungal strains for amylase production." New Biotechnology 25 (September 2009): S73. http://dx.doi.org/10.1016/j.nbt.2009.06.318.
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Arakawa, Tsutomu, Lynne Hung, and Linda O. Narhi. "Stability of fungal ?-amylase in sodium dodecylsulfate." Journal of Protein Chemistry 11, no. 2 (April 1992): 111–17. http://dx.doi.org/10.1007/bf01025216.
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Essiedu, Justice Amakye, Frank Seth Johnson, and Francis Ayimbila. "ISOLATION OF AMYLASE PRODUCING FUNGI FROM CASSAVA FLOUR." Fungal Territory 4, no. 1 (March 17, 2021): 5–9. http://dx.doi.org/10.36547/ft.151.
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Amylases are among the most important enzymes with potential applications in the present-day industry. Thus, isolating pure culture from cassava as the cheap source has manifold importance for food industries. In the present study, eleven amylase producing fungal strains were isolated from cassava flour and growth pattern, as well as optimum growth condition, was determined. All isolates showed amylases activity but isolate BR005, BR001 and GR003 recorded maximum clear zone diameters of 54.75 ± 0.957 mm, 53.25 ±0.645 mm 51.5 ± 1.414 mm, respectively. The submerged fermentation method was employed for crude amylase and biomass production. There were significant differences (p˂0.05) in starch concentrations and growth rates between the three isolates. GR003 and BR005 attained their optimal amylase activities of 4.23±0.25 U/mL and 3.75±3.16 U/mL at 50 °C, respectively, whiles BR001 attained its optimum amylase activity of 3.43±0.77 at 60 °C. Whereas, BR005, BR001 and GR003 attained their optimal amylase activity of 5.14±1.99 U/mL, 4.53±0.01 U/mL and 1.25±1.11 U/mL at a pH range of 6 to 7, making them neutrophilic fungi. Moreover, isolates BR005, BR001 and GR003 recorded the highest amylase activities of 4.31±0.14U/mL, 4.67±1.16±U/mL and 3.16±0.12U/mL at the starch concentrations of 3%, 2%, and 2.5% and fermentation period of 48 h, 66 h and 42 h, respectively. Lastly, BR005, BR001 and GR003 achieved their optimal amylase activities of 5.41±0.11U/mL, 6.24±0.14 U/mL and 6.22±0.12 U/mL at 48 h, 66 h and 42 h of incubation, accordingly. Indicating that cassava flour is a good source of amylolytic fungi with a potential application under wide conditions.
Dissertations / Theses on the topic "Fungal amylase"
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Strait, Matthew John. "The Effect of Liquid or Dry Honey as a Partial Replacement for Sugar on the Baking and Keeping Qualities of Fat Reduced Muffins." Thesis, Virginia Tech, 1997. http://hdl.handle.net/10919/36875.
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The food industry has responded to the American Heart Association's overwhelming concerns about the complications of obesity with an array of fat reduced products that maintain the functionality of fat in given systems. In baked products, it appears that no one single ingredient effectively mimics these functions. The present study investigated the effect of liquid or dry honey as a partial replacement for sugar on the baking and keeping qualities of fat reduced muffins. The fat reduced muffins also utilized a hydrocolloid fat replacer, bacterial and fungal amylases, and an emulsifier (DATEM).
Results showed that both liquid and dry honey significantly (p<0.05) increased crust and crumb color at all replacement levels, however the use of 25% liquid honey was shown to favorably increase the crust color of fat reduced muffins. Volume was not significantly (p>0.05) affected but appeared to decrease with the addition of honey due to either premature starch gelatinization or a decrease in batter pH. The addition of honey increased moisture content, and decreased water activity, but did not decrease firmness or staling rates especially after prolonged frozen storage. Sensory panelists noted that the addition of liquid or dry honey increased the cohesive forces and decreased tenderness. The addition of moisture to the fat reduced system did not appear to improve the perceived moistness of the product.Master of Science
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Ferreira, Osania Emerenciano. "Aproveitamento de subprodutos agroindustriais para a produção de amilases fúngicas : estudo de parâmetros fermentativos e caracterização das enzimas /." Jaboticabal : [s.n.], 2011. http://hdl.handle.net/11449/94886.
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Orientador: Márcia Rossini Justino MuttonBanca: Eduardo da Silva Martins
Banca: João Martins Pizauro Júnior
Resumo: A utilização de fermentação em estado sólido a partir de subprodutos agroindustriais possibilita a obtenção de várias biomoléculas de interesse industrial. As amilases são enzimas com grande aplicação nas indústrias têxtil, farmacêuticas, alimentícias e sucroalcooleira, representando aproximadamente 25% do mercado mundial. Neste trabalho foram isoladas três linhagens fúngicas (Rhizopus oryzae, Malbranchea pulchella e Chrysosporium zonatum), que apresentaram potencial amilolítico, quando cultivadas em três resíduos agroindustriais (quirera de arroz e de milho e farelo de trigo). Para a cepa que apresentou maior atividade enzimática, avaliou-se melhor substrato, tempo de cultivo, teores de umidade, fontes suplementares de nitrogênio, pH e temperatura de incubação, objetivando otimizar as condições de cultivo. Observou-se que a maior atividade enzimática foi obtida com a cepa de R. oryzae em 24 horas de fermentação, em meio de cultura contendo farelo de trigo como substrato, em temperatura de 35°C, utilizando solução de sais composta de NH4NO3 a 0,1% e MgSO4.7H2O a 0,1% como fonte de nitrogênio. Alterações de pH entre 4,0 e 6,0 não afetaram significativamente a síntese da enzima. A condições ótimas de atuação foram temperatura de 75°C e pH de 4,5. As enzima manteve-se estável a 75°C na ausência de substrato por 25 minutos
Abstract: The use of fermentation in a solid state from agroindustrial byproducts permits the obtaining of several biomolecules of interest the industry, like the enzymes. The amylases are enzymes with great application on the textile, pharmaceutical and food industries, representing around 25% of the worldwide market. In this work three ungal strains (Rhizopus oryzae, Malbranchea pulchella and Chrysosporium zonatum) were isolated. They presented amylolytic potential when cultivated in three agroindustrial by products (brewers rice, corn grits and wheat bran). To the strain that presented the greatest enzyme activity, it was evaluated the best substrate, cultivation time, moisture content, additional sources of nitrogen, pH and incubation temperature, aiming the optimization of cultivation conditions. I was observed that the greatest enzyme's activity was obtained with 24 hours of fermentation, in R. orizae in a culture medium that contained wheat bran as the substrate, at 35°C, using salt solution made with NH4NO3 0.1%, MgSO4.7h2O 0.1% and (NH4)2SO4 0.1% as nitrogen source. pH alterations between 4.0 and 6.0 didn't change significantly the enzyme's activity. The optimum conditions of performance of the enzyme were temperature of 75°C and pH 4.5. The enzyme kept stable in the lack of substrate for 25 minutes in 75°C
Mestre
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Ferreira, Osania Emerenciano [UNESP]. "Aproveitamento de subprodutos agroindustriais para a produção de amilases fúngicas: estudo de parâmetros fermentativos e caracterização das enzimas." Universidade Estadual Paulista (UNESP), 2011. http://hdl.handle.net/11449/94886.
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ferreira_oe_me_jabo.pdf: 412993 bytes, checksum: aae1d57cd30b58d78f8d841727177cc0 (MD5)A utilização de fermentação em estado sólido a partir de subprodutos agroindustriais possibilita a obtenção de várias biomoléculas de interesse industrial. As amilases são enzimas com grande aplicação nas indústrias têxtil, farmacêuticas, alimentícias e sucroalcooleira, representando aproximadamente 25% do mercado mundial. Neste trabalho foram isoladas três linhagens fúngicas (Rhizopus oryzae, Malbranchea pulchella e Chrysosporium zonatum), que apresentaram potencial amilolítico, quando cultivadas em três resíduos agroindustriais (quirera de arroz e de milho e farelo de trigo). Para a cepa que apresentou maior atividade enzimática, avaliou-se melhor substrato, tempo de cultivo, teores de umidade, fontes suplementares de nitrogênio, pH e temperatura de incubação, objetivando otimizar as condições de cultivo. Observou-se que a maior atividade enzimática foi obtida com a cepa de R. oryzae em 24 horas de fermentação, em meio de cultura contendo farelo de trigo como substrato, em temperatura de 35°C, utilizando solução de sais composta de NH4NO3 a 0,1% e MgSO4.7H2O a 0,1% como fonte de nitrogênio. Alterações de pH entre 4,0 e 6,0 não afetaram significativamente a síntese da enzima. A condições ótimas de atuação foram temperatura de 75°C e pH de 4,5. As enzima manteve-se estável a 75°C na ausência de substrato por 25 minutos
The use of fermentation in a solid state from agroindustrial byproducts permits the obtaining of several biomolecules of interest the industry, like the enzymes. The amylases are enzymes with great application on the textile, pharmaceutical and food industries, representing around 25% of the worldwide market. In this work three ungal strains (Rhizopus oryzae, Malbranchea pulchella and Chrysosporium zonatum) were isolated. They presented amylolytic potential when cultivated in three agroindustrial by products (brewers rice, corn grits and wheat bran). To the strain that presented the greatest enzyme activity, it was evaluated the best substrate, cultivation time, moisture content, additional sources of nitrogen, pH and incubation temperature, aiming the optimization of cultivation conditions. I was observed that the greatest enzyme’s activity was obtained with 24 hours of fermentation, in R. orizae in a culture medium that contained wheat bran as the substrate, at 35°C, using salt solution made with NH4NO3 0.1%, MgSO4.7h2O 0.1% and (NH4)2SO4 0.1% as nitrogen source. pH alterations between 4.0 and 6.0 didn’t change significantly the enzyme’s activity. The optimum conditions of performance of the enzyme were temperature of 75°C and pH 4.5. The enzyme kept stable in the lack of substrate for 25 minutes in 75°C
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Canterella, Robin L. "The influence of selected bacterial and fungal enzymes on the baking and keeping quality of a fat substituted muffin." Thesis, This resource online, 1995. http://scholar.lib.vt.edu/theses/available/etd-06112009-063915/.
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Wu, Caiyan. "Developing Ophiostoma floccosum as a novel expression system." Australia : Macquarie University, 2007. http://hdl.handle.net/1959.14/291.
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"This thesis is based on the following articles, referred to in the text by the Roman numerals given below. In addition some unpublished results are presented. I. Caiyan Wu ... [et al] Improvement of the secretion of extracellular proteins and isolation and characterization of the amylase I (amyI) gene from Ophiostoma floccosum [pub. in ] Gene 384: 96-103 -- II. Caiyan Wu ... [et al.] Activity-based identification of secreted serine proteases of the filamentous fungus Ophiostoma. Accepted by Biotechnology letters DOI 10.1007/s10529-007-9333-6 -- III. Caiyan Wu ...[et al.] Expression of a thermostable bacterial xylanase in the filamentous fungus Ophiostoma floccosum. Submitted to Letters in applied microbiology in July 2007." - leaf 9.Thesis (PhD)--Macquarie University, Division of Environmental and Life Sciences, Dept. of Chemistry & Biomolecular Sciences, 2007.
Bibliography: leaves 100-123.
Introduction -- Materials and methods -- Results and discussion -- Conclusion and future aspects -- References -- Publications I, II and III.
Ophiostoma spp. belong to the Ophiostomataceae family, a large group of ascomycetes, which are the most frequent blue stain fungi isolated from stained wood. Most Ophiostoma species do not compromise the strength properties of wood, but do reduce the aesthetic quality of timber and therefore decrease the economic value of lumber. Some albino variants of O. floccosum and O. piliferum have been used as biological control agents to prevent blue staining. This successful whole organism approach plus the added capability of extracellular protein secretion makes Ophiostoma spp. attractive for industrial application. In addition, Ophiostoma produces only a small range of abundantly secreted proteins in liquid culture, which can facilitate downstream purification of any recombinant gene product introduced into the system. Genes encoding efficiently secreted proteins provide a potential souce for strong promoters for high-level gene expression. These characteristics provide an excellent starting point for the development of a novel expression system.
In this study, UV-mutagenesis was applied to improve protein secretion in Ophiostoma floccosum. Amylase activity was used as an indicator for enhanced protein secretion after repeated rounds of mutagenic treatment. Several mutants of O. floccosum derived by UV mutagenesis were isolated and the total amount of secreted protein was increased by 4 to 6 times. The amylase activity in the culture supernatant of the best mutant (MQ.5.1) was increased by more than 240-fold compared to the initial parental strain. At the same time, the amount of total secreted protein was about six times greater to that of the parental strain. Proteinase profiles in the culture supernatants of several key mutants were characterized for the future matching of an expression host with a particular gene product. N-terminal sequencing of the five dominant proteins separated by SDS-PAGE from the culture supernatant was conducted. Two of the proteins identified were subtilisin-like proteinases and one was a pepsin-like proteinase. In addition, one protein was identified as an_-amylase and one remained unidentified. A 6.5 kb DNA fragment was isolated by Genomic Walking PCR using primers based on the _-amylase amino acid sequence. The amplified fragment contained the entire gene encoding_-amylase (amyl) and its regulatory sequences. Analysis showed that multiple transcripts were generated from the single _-amylase gene locus.
A series of expression vectors containg the _-amylase regulatory sequences and partial amyl gene were constructed. Several selection markers were screened and the hph gene conferring hygromycin resistance under the regulation of the Aspergillus nidulans gpd promoter was chosen and inserted into the amyl expression vectors. The gene encoding a red fluorescent protein DsRed-E5 was used as a reporter gene to test the expression system using mutant MQ.5.1 as host. However, no transformants were obtained by either biolistic transformation or protoplast transformation. Subsequently, an alternative strategy was developed using a thermostable xylanase B as a reporter. Thermostable xylanase activity was detected in the culture supernatants of several transformants. Production of xylanase by transformant SS41 which exhibited high secreted xylanase activity was investigated. Xylanase activity in the culture supernatant of SS41 was visualized by a zymogram gel assay. Two active proteins with molecular masses of around 27 and 30 kDA, which were larger than the predicted Mr of 25 kDA were detected. This is the first report describing successful expression of a recombinant thermostable bacterial enzyme in Ophiostoma.
Mode of access: World Wide Web.
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Almeida, Paula Zaghetto de. "Diversidade do potencial amilolítico em fungos filamentosos: purificação e caracterização de uma glucoamilase de Aspergillus brasiliensis." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/59/59139/tde-15052015-085904/.
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O Brasil apresenta cerca de 10 a 17,6% da biodiversidade mundial e apenas uma fração dela é conhecida. Os fungos filamentosos são bons produtores de enzimas e despertam um grande interesse biotecnológico. O amido é o principal carboidrato de reserva das plantas. Dentre as enzimas amilolíticas estão as glucoamilases, que catalisam a hidrólise das ligações -1,4 e -1,6 das extremidades da cadeia do amido liberando glucose. Neste trabalho foram isolados 25 fungos filamentosos de amostras de materiais em decomposição da Mata Atlântica. Dos micro-organismos com alta atividade amilolítica foram selecionados e identificados Aspergillus brasiliensis e Rhizopus oryzae. Foi realizada a otimização do cultivo e caracterização das amilases do extrato bruto de ambos os fungos. Após a obtenção destes dados foi selecionado A. brasiliensis, pois, sua amilase é mais termoestável e ainda não reportada na literatura. Após purificação a enzima foi identificada como glucoamilase, a qual é monomérica com 69 kDa e contém aproximadamente 21% de carboidratos. Apresenta um domínio de ligação ao amido na porção terminal e estrutura secundária rica em -hélice. Sua atividade ótima ocorre em pH 4,5 a 60°C, seu pI é de 3,21, pode ser ativada com a adição de Mn2+, e é inibida por glucose em concentrações maiores que 0,1 M. A glucoamilase apresenta excelente estabilidade ao pH e boa estabilidade a temperatura (a 50°C mantém 67% de atividade após 7 horas; a 55°C a meia vida é de 147 minutos). Com amido de batata a enzima apresentou as seguintes constantes cinéticas (km 2,21 mg/mL; Vmáx 155 U/mg; kcat 179 s-1; kcat/km 81,06). A glucoamilase foi imobilizada em DEAE-PEG com ativação de 12 vezes e possibilidade de reuso de 10 vezes com perda de apenas 31% de atividade. O derivado demostrou maior facilidade para hidrolisar a amilopectina do que à amilose. Também foi realizada uma análise de neighbor joining, que agrupou a glucoamilase de A. brasiliensis próxima às glucoamilases de espécies de Aspergillus, que são consideradas as mais derivadas.Brazil holds about 10-17.6% of the world\'s biodiversity and just a percentage of it is known. Filamentous fungi are enzyme producers that have great biotechnological application. Starch is the main reserve carbohydrate in plants. Among the amylolytic enzymes there are the glucoamylases, that catalyze the hydrolysis of -1,4 and -1,6 linkages of the end of starch chains, and releases glucose. In this research 25 filamentous fungi from Atlantic forest decaying material samples were isolated. Among microorganisms with high amylolytic activity Aspergillus brasiliensis and Rhizoupus oryzae were selected and identified. The cultivation parameters were optimized and the enzymes of crude extract were characterized. Considering the previous data Aspergillus brasiliensis was selected because its amylases are more thermostable and it has not been described in the literature yet. After purification the enzyme was identified as a glucoamylase, which is monomeric with 69 kDa and about 21% of carbohydrates in its composition. The enzyme has a starch binding domain in the terminal position and its secondary structure is rich in -helix. The optimum pH for glucoamylase activity is 4.5, the temperature is 60ºC and its pI is 3.21. The enzyme can be activated by the addition of Mn+2, and inhibited in concentrations above 0,1M glucose. The glucoamylase has an excellent pH stability and a good temperature stability (at 50ºC 67% of the activity was retained after 7 hours; at 55°C its half-life was 147 minutes). The best kinetic values were obtained with potato starch (km 2.21 mg/mL; Vmax 155 U/mg; kcat 179 s-1; kcat/km 81,06). The glucoamylase was immobilized on DEAE-PEG, with an activation of 12 times and enzyme reuse 10 times with just 31% loss of its activity. The immobilized enzyme has a greater activity on amylopectin than amylose. A neighbor joining analysis with glucoamylases from filamentous fungi species was made and Aspergillus brasiliensis glucoamylase was grouped close to the glucoamylases of Aspergillus species, which are considered the most derivative.
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Mishra, Ravi Shankar. "Amylases From A Thermophilic Fungus Thermomyces Lanuginosus Iisc 91 :Their Purification And Properties." Thesis, Indian Institute of Science, 1994. http://hdl.handle.net/2005/90.
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A knowledge of molecular properties and structure of heat-stable enzymes is important for the understanding of basic principles governing thermo stability of proteins and evolution of life at high temperatures. Information on functional characteristics of thermo stable enzymes is necessary also for improving existing biotechnologies and developing new ones. Because of these reasons enzymes from thermophilic organisms are being exploited. In this context, amylolytic enzymes represent a useful choice for investigation from both basic and applied points of view.
a-Amylase and glucoamylase hydrolyse starch into oligosaccharides and glucose, respectively. In the present study a thermophilic fungus, Thermomyces lanuginosus, was selected as a source of thermostable starch-degrading enzymes. The main objectives of this research were to understand the physicochemical properties, mechanism of starch utilization by T. lanuginosus and effect of heat, on amylo1ytic enzymes.
Purification of amylolytic enzymes
A strain of T, lanuginosus, IlSc 91, isolated from a manure heap in our laboratory was found to produce higher levels of extra cellular amylolytic enzymes than strains obtained from culture collection in U.S.A, and Europe. This strain produced 4 units of glucoamylase and 40 units of a-amylase per ml of culture filtrate when grown on 2% starch at 50 C. Culture filtrate was used as the starting material for purification of these enzymes. Glucoamylase and a-amylase were purified by ultrafiltration and a combination of ion exchange and gel-filtration chromatography 93- and 112-fold with 30 and 41% recovery, respectively; Homogeneity of purified enzymes was established by the criteria of native- PAGE, SDS-PAGE, gel-filtration on HPLC and N-terminal amino acid analysis. Some of the physicochernical properties of these enzymes were studied.
Physicochemical characteristics
Glucoernylase is a monomeric glycoprotien (carbohydrate content 11 %, w/w) and has a molecular weight, of 45 kDa. It produces only glucose from starch. Km and Vmax, for soluble potato starch are 0.04 mg ml-1 and 666 p mole glucose min-1 mg protein-1, respectively. The enzyme is optimally active at 70 C at pH 6.0. Its activation energy is 14.0 kCal mole-1. It has melting temperature of 73 C. Molar extinction coefficient of glucoamylase is 5.5 x 104 mole-1 cm-l. It is stable at 60°C for > 7h. The enzyme is rich in alanine, serine and aspartate/ asparagine. Glucoamylase contains alanine as the N-terminal amino acid. It does not contain cysteine.
Purified a-amylase is a homodimeric protein of 40 kDa and contains 5% (w/w) carbohydrate. It liberates oligosaccharides from starch with maltose being the principle product of hydrolysis. The Km for soluble starch is 2.5 mg ml-1. A high Vmax, of 8000 mg starch min-1 mg protein-1 was found. The enzyme is optimally active at 65°C at pH 5.6. The activation energy is 10.9 kCal mole-1. At 50DC, which is the optimal temperature of growth of T. lanuginosus, purified a-amylase is completely stable for over 6 h. Ca2+ increases the melting temperature of a-amylase from 66°C to 73°C. a-Amylase requires Ca2+ for its activity and structural stabi1it.y The molar extinction coefficient of the enzyme is 4.7 x 10' mole-1 cm-1 a- Amylase is rich in aspartate / asparagine, glutamatme /glutamine, alanine, glycine and leucine. It does not contain cysteine. a- Amylase contains alanine as the N-t.ermina1 amino acid.
Hydrolysis of starch by a-amylase and glucoamylase
Experiments were done to understand the role of a-amylase and glucoamylase in the
utilization of starch by T. lanuginosus. Crude and purified amylase preparations hydrolyse raw potato starch slightly more efficiently than soluble potato starch. The extent of starch hydrolysis by a mixture of a-amylase and glucoamylase is equal to that by culture filtrate containing the same amount of enzyme activities, Electrophoresis of crude culture filtrate proteins on native-PAGE and activity staining on gel showed the presence of one species each of a-amylase and glucoamylase. This suggests that in T. lanuginosus hydrolysis of starch is mediated by one species each of extracellular a-amylase and glucoamylase. The hydrolysis of starch by a mixture of a-amylase and glucoamylase is equal to the arithmetic sum of hydrolysis by individual enzyme showing that the enzymes do not act synergistically. a-Amylase is the main starch depolymerizing enzyme. Conversion of starch into glucose by glucoamylase does not require the presence of a-amylase. Starch is hydralysed to a maximum of 72 and 97% by glucoamylase and a-amylase, respectively.
Effect of heat on a-amylase
The effect, of heat, on a-amylase and glucoamylase was studied with the view to obtain information on the thermal inactivation of these proteins. Five-min heat treatment of the native a-amylase (40 kDa) results in the specific conversion of all protein molecules into partially active (approximately 50% residual activity) and SDS-undissociable dimer of 45 kDa. a-Amylase (45 kDa) after 5-min heat treatment. is partially active and can he rendered completely active by incubation at 37°C for 3 h. This altered form of a-amylase is not due to the formation of disulfide linkage in protein because the enzyme does not contain cysteine and b mercaptoethanol does not prevent heat-induced structural change. Heat, treatment, for 20 min or more results in further structural changes which result in the irreversible inactivation of the enzyme. Prolonged heating (>40 min) probably causes the degradation of protein. Reactivation of 20-min heat-inactivated a-amylase occurs specifically at 37°C or 50°C within 3 h but not at lower temperatures (0°C or 4°C). Native-PAGE analysis of the native and 20-min heated-reactivated a-amylase shows that the reactivated sample is comprised of two protein species of different charge and/or mass. Activity staining shows that only one of these protein band is active and it has electrophoretic mobility identical to that of the native enzyme. Native and the active fraction of 20-min heated-reactivated a-amylase possess similar specific activity. This suggests that it is cat8alytmically and perhaps structurally similar to the native enzyme. The native and the reactivated a-amylase are resist ant to trypsin digestion. However, heat- inactivated a-amylase is degraded into low molecular weight, peptides. These observation suggest that heat-inactivated a-amylase is partially unfolded, Unlike the native, the heat-treated (94"C, 5 min) a-amylase can not be stained with AgN03 while both forms can be stained with Coomassie brilliant blue R and by Schiff's base. On the basis of these observations a tentative model was proposed for the effect of heat on a-amylase (Fig.)
Staining by + +
Staining by AgNO3, + +
Staining by Schiff 's base + +
Sensitivity to trypsin + +
Figure : Schematic represent ation of heat-induced changes in a-amylase
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Freitas, Patricia Rabelo de. "EFEITO DE ENZIMAS AMILOLÍTICAS DE Aspergillus awamori SOBRE A DIGESTÃO DO AMIDO EM BOVINOS." Pontifícia Universidade Católica de Goiás, 2012. http://localhost:8080/tede/handle/tede/2501.
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Previous issue date: 2012-05-15Avaliou-se o efeito de uma solução de amilase produzida por Aspergillus awamori sobre a digestibilidade in vitro da matéria seca (DIVMS) de milho. Foram realizados dois experimentos, onde o primeiro a solução de enzima amilase foi aplicada por pulverização em 24g de milho moído (2 mm) e o segundo a solução de enzima amilase foi aplicado no fluido ruminal. Os tratamentos foram: controle (0 enzima), T1 (5Ml de enzima) e T2 (10Ml de enzima) para cada experimento. O ensaio da DIVMS foi obtido usando a técnica de rúmens artificiais adapatada durante os períodos de 15 ; 1,30 , 3, 6, 12 e 24 horas. Para a coleta de líquido ruminal foi utilizado um bovino de peso aproximado de 380 kg. O animal foi mantido em baia e adaptado a dieta durante um período de 10 dias antes do recolhimento do líquido ruminal com acesso livre à água e sal mineral. Para os dois experimentos foi adotado o delineamento inteiramente casualizado, em esquema de parcelas subdivididas 3 x 6, com quatro repetições (jarros). As parcelas foram constituídas por milho tratado com três diferentes níveis de enzima e as subparcelas por seis momentos de digestão. Para enzima amilase aplicada no líquido ruminal o resultado de DIVMS para os três tratamentos nos períodos de 3, 6 e 12 horas não diferiram estatisticamente entre si. Entre o tratamento controle e T1 houve diferença significativa nos tempos 15 e 1,30 horas. Foi observado maior DIVMS para o tratamento controle, em relação ao T1, com valores de 54,54% e 49,05 , e não houve diferença nos tempos 3, 6, 12 e 24 horas. Entre o tratamento controle e T2 não houve diferença no tempo 15 e 24 horas. O controle foi superior a T2 28,74% e 10,53%, respectivamente. A DIVMS foi superior para o tratamento controle, indicando que os níveis de 5 e 10 ml de enzimas injectados no fluido ruminal não aumentaram a DIVMS. Para amilase aplicada por pulverização em 24g de milho moído, no tempo de 15 , observou-se que o tratamento controle e T1 não diferiram. No entanto, o T2 melhorou a DIVMS em 55,54%, comparado ao grupo controle. O tratamento T1 aumentou a DIVMS apenas em tempos de 3 e 24 horas de incubação, em relação ao controle. Com a aplicação de 10 ml de enzima, a DIVMS aumentou em todos os tempos de incubação, em comparação com o controle.
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Costa, Beatriz de Oliveira [UNESP]. "Efeito da inoculação de fungos na atividade enzimática de solos e germinação de sementes de milho." Universidade Estadual Paulista (UNESP), 2010. http://hdl.handle.net/11449/88327.
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costa_bo_me_jabo.pdf: 5899495 bytes, checksum: c015de9c632910013a84b4f478dbde40 (MD5)O conhecimento da atividade das enzimas hidrolíticas é essencial para compreender as transformações dos nutrientes no solo. O milho é uma das principais culturas sob o ponto de vista econômico. O objetivo deste estudo foi avaliar a influência do crescimento dos fungos em dois tipos de solos, na presença e ausência de glicose, no desenvolvimento das plântulas de milho, no padrão isoenzimático dos coleóptilos, nos teores de carboidratos totais residuais, nas atividades da desidrogenase e amilase. Utilizou-se delineamento inteiramente casualizado com esquema fatorial. A adição de glicose no meio de cultura aumentou a velocidade de crescimento de A. flavus e Penicillium sp., mas não de F. verticillioides. Na presença de glicose, a produção de esporos aumentou de 1,2 (F. verticillioides) e 8,2 vezes (A. flavus), e reduzido de 3,5 vezes com Penicillium sp. A redução dos teores de carboidratos totais ajustou-se significativamente às equações de 1º e 2º grau. A.flavus e Penicillium sp., apresentaram maior consumo de carboidratos totais que o solo sem inoculação ou inoculado com F. verticillioides. A adição de glicose no solo favoreceu o consumo de carboidratos residuais, provavelmente devido ao estímulo do crescimento dos fungos. Exceto com F. verticillioides, a atividade da desidrogenase aumentou em média de 1,5 a 1,8 vez (p<0,05) nos solos com glicose em relação aos solos sem glicose. À atividade da amilase, aumentou 1,3 a 1,5 vez por efeito da adição de glicose no solo. Maior atividade da amilase foi observada no solo Latossolo Vermelho distrófico (LVd) com glicose e inoculado com A.flavus e Penicillium sp. em relação ao controle. As dimensões das plântulas como altura dos coleóptilos, comprimento das raízes e massa seca das plântulas de milho dos solos adicionados de glicose e/ou inoculados com os fungos foram diminuídas. A expressão genética...
The knowledge about hydrolytic enzymes activity is essential to understand the nutrients transformations in soil. Corn is one of the main crops from the economic view in the whole world. The objective of this study was evaluate the fungi growth in two soil types, in the presence and absence of glucose, coleoptiles development, roots and weight of corn seedlings, coleoptiles isoenzyme pattern, content of total residual carbohydrates, enzymes dehydrogenase and amylase activity. Was used a completely randomized design with factorial arrangement. The glucose addition in culture medium increased the growth rate of A. flavus and Penicillium sp., but not F. verticillioides. In the presence of glucose, the spores number was increased from 1.2 (F. verticillioides) and 8.2 times (A. flavus), but was reduced 3.5 times with Penicillium sp. Reducing the levels of total carbohydrates, significantly adjusted to the equations of 1st and 2nd grade. A.flavus and Penicillium sp., showed higher carbohydrates consumption that the soil control or inoculated with F. verticillioides. The glucose addition in soil, favored the use of residual carbohydrates, probably due fungi growth stimulation. Except F. verticillioides, dehydrogenase activity increased in the range 1.5 to 1.8 times (p<0.05) in soils with glucose compared to glucose free soil. Amylase activity increased 1.3 to 1.5 times by glucose addition effect in soil. Increased amylase activity was observed in the Distrophic Red Latosol (DRL) with glucose and inoculated with A.flavus and Penicillium sp., compared to control. The seedlings dimensions as coleoptiles height, root length and dry weight of maize seedlings of the soils added with glucose and inoculated with fungi were decreased. Gene expression of maize seed was changed due probable by fungi inoculated infection in soil. The coleoptiles isoenzymes pattern was amended as early as 5 incubation... (Complete abstract click electronic access below)
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Guandalini, Natalia Capeletti. "Estudo da produção de enzimas amiloliticas pelo fungo Metarhizium." [s.n.], 2007. http://repositorio.unicamp.br/jspui/handle/REPOSIP/255479.
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Orientador: Ranulfo Monte Alegre, Vanildo Luiz Del BianchiDissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos
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Resumo: O fungo Metharhizium anisopliae tem sido empregado no biocontrole de insetos em diferentes regiões do Brasil, com aplicação principal em lavouras de cana-de-açúcar. O processo de biocontrole envolve a adesão dos esporos do fungo à superfície do inseto, a destruição do mesmo através da pressão mecânica das hifas, além de processos de digestão enzimática de proteínas, quitinas e lipídeos. Por esse motivo, estudos indicam a viabilidade da produção de amilases, proteases, lipases e quitinases pelo fungo. Além disso, este fungo tem sido objeto de estudos como produtor de swainsonine, um alcalóide com ação potencial na inibição da metástase celular e do crescimento primário de tumores, sendo promissora a sua utilização em tratamentos contra o câncer e AIDS. Sendo assim, este trabalho teve como objetivo estudar o potencial amilolítico de linhagens de Metarhizium anisopliae. Para a produção das enzimas utilizou-se fermentação em meio sólido. Para tanto, o microrganismo mantido em meio BDA foi inoculado através da suspensão de células na concentração de 107 esporos/g em 10 g de meio farelo e casca de arroz, em proporções de 7/3 (p/p), 6/4 (p/p) e 8/2 (p/p). A umidade inicial dos meios de cultivo variou em 47%, 65% e 74%. A fermentação ocorreu em sacos de polipropileno, os quais foram mantidos a 28ºC durante 480 horas, sendo retiradas amostras a cada 24 horas. No extrato enzimático obtido foram determinadas as atividades de a-amilase e de amiloglicosidase. Para o estudo da influência da interação de fatores como meio de cultivo, umidade, pH e concentração de esporos na produção das enzimas em estudo, foi utilizado um planejamento experimental 24-1, onde se observou que o pH apresenta influência na produção de a-amilase. Para a produção de a-amilase e amiloglicosidase, observou-se que o melhor meio de cultivo foi o constituído por farelo e casca de arroz na proporção 6/4 (p/p), com umidade de 47%. O pH ótimo para a atividade de a¿amilase e de amiloglicosidase foi de 5 - 5,5, apresentando estabilidade numa faixa de 5 ¿ 6,5 para a a¿amilase e de 5,5 ¿ 6 para a amiloglicosidase. A temperatura ótima para a atividade enzimática de a¿amilase foi de 70ºC e de 60ºC para a amiloglicosidase, apresentando estabilidade numa faixa de 10 a 50ºC. A atividade enzimática de a¿amilase foi influenciada positivamente pelos íons Mg+2, Mn+2, K+, Ca+2 e EDTA, enquanto o íon Zn+2 influenciou negativamente a atividade da enzima. Para a amiloglicosidase, todos os íons testados apresentaram efeito negativo, com destaque para o Zn+2 que apresentou a maior redução na atividade enzimática
Abstract: The fungus Metharhizium anisopliae has been used as biocontrol agent, actuating on insects in different areas of Brazil, with main application in sugarcane farmings. Such a biocontrol process involves the adhesion of the fungus spores to the surface of the insect, destruction of the same through the mechanical pressure of the hyphal, as well the processes of enzymatic digestion of proteins, chitins and lipids. For that reason, studies indicate the viability of the production of amylases, proteases, lipases and chitinases by this fungus. Besides, it is object of studies as producer of swainsonine, an alkaloid with potential action in the metastasis cellular and in the primary growth of tumors, being promising its use in treatments against the cancer and AIDS. The objective of this work was to evaluate the amylolytic potential of the strains of Metharizium anisopliae. For the enzymes production, it was utilized solid state fermentation. For that, the microorganism maintained in PDA media was inoculated through the suspension of cells in the concentration of 107 spores/g in 10 g of media constituted by bran and rice chaff, in proportions of 7/3 (p/p), 6/4 (p/p) and 8/2 (p/p). The initial moisture content of fermentation was varied on 47%, 65% and 74%. The experiments were carried in polypropylene bags, which were incubated at 28ºC for 480 hours of fermentation, being removed from it, samples every 24 hours. From the crude enzymatic solution, there were determined the activities of a-amylase and the amiloglucosidase. For the study of the interaction of factors such as cultivation medium, moisture, pH and inoculum size in the enzymes production, a statistical design 24-1 was used, where it was observed that the pH presents influence in the production of a-amylase. For the production of a-amylase and amiloglicosidase, it was concluded that the best cultivation medium is constituted by bran and rice chaff in the proportion 6/4 (p/p), with a moisture content of 47%. The optimum pH for a-amylase and amiloglicosidase was of 5 - 5,5, presenting stability in a pH range from 5 to 6,5 for the a- amylase and 5,5 to 6 for the amiloglicosidase activity. The best temperature for a-amylase activity was 70ºC and 60ºC for the amiloglicosidase, presenting stability in a range from 10 to 50ºC. The a-amylase activity was influenced positively by the ions Mg+2, Mn+2, K+, Ca+2 and EDTA, while the ion Zn+2 influenced negatively the enzyme activity. For the amiloglicosidase, all of the tested ions presented negative effect, with prominence for Zn+2 that presented the largest reduction in the enzymatic activity
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Mestre em Engenharia de Alimentos
Books on the topic "Fungal amylase"
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Smith, Stephanie J., Rohini J. Manuel, and Christopher C. Kibbler. Aspergillus species. Edited by Christopher C. Kibbler, Richard Barton, Neil A. R. Gow, Susan Howell, Donna M. MacCallum, and Rohini J. Manuel. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198755388.003.0010.
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There are more than 200 Aspergillus species, with over 30 known to be human pathogens. The fungus is also commercially important. Aspergillus niger is the source of enzymes such as amylases, lipases, and proteases and is used to produce the majority of the world’s citric acid. Diseases caused by Aspergillus species can vary widely, from superficial colonization to invasive and allergic disease. Mortality from invasive disease remains high, despite an increase in the number of antifungals available for therapy. Azole resistance is increasing, especially in Europe, and appears to be related to the use of azoles for agriculture.
Book chapters on the topic "Fungal amylase"
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Mazzoli, Roberto, and Enrica Pessione. "Ancient Textile Deterioration and Restoration: Bio-Cleaning of an Egyptian Shroud Held in the Torino Museum." In Microorganisms in the Deterioration and Preservation of Cultural Heritage, 199–216. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-69411-1_9.
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AbstractAncient textiles are fragile and several factors can affect their integrity. In the present chapter, the main agents of deterioration of old and new textiles, namely physical-chemical (light, oxygen, heat, and humidity) and biological factors as well as human erroneous interventions will be explored. As far as the biological deterioration is considered, the effects of microbial growth, primary and secondary metabolites (acids, solvents, surfactants, pigments) and enzymes (lipases, proteases, and glycosidases) on textile strength and cleanliness will be described in details. The main fungal and bacterial species involved in the damage (textile discoloration, black and green spots, cuts) will be reported. Adhesive application during restoration procedures is discussed to highlight the risk of glue thickening giving rise to dull precipitates on the fabric.The main strategies for oil-stain and glue removal (both animal glue, such as fish collagen, and vegetal glue, i.e. starch) will be described in the paragraph devoted to biorestoration. Finally, a case study concerning an ancient Coptic tunic housed in the Egyptian Museum of Torino, Italy, and biocleaned by means of gellan-immobilized alpha-amylase from Bacillus sp. will be largely discussed by reporting historical data, adhesive characterization, methods for artificial aging of simulated sample and glue removal from the artwork.
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Jensen, B., J. Olsen, and K. Allermann. "Extracellular Amylase from the Thermophilic Fungus Thermomyces Lanuginosus." In Extracellular Enzymes of Microorganisms, 143–46. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1274-1_18.
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Alves do Prado, Heloiza, Aline dos Reos, Erica Santos, and Raisa Sanches. "Fungal Amylase." In Fungal Enzymes. CRC Press, 2013. http://dx.doi.org/10.1201/b15247-18.
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Technical, AACC. "Measurement of alpha-Amylase Activity in Flour Supplemented with Fungal alpha-Amylase--Modified Amylograph Method." In AACC International Approved Methods. AACC International, 2009. http://dx.doi.org/10.1094/aaccintmethod-22-12.01.
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Cripwell, Rosemary A., Willem Heber van Zyl, and Marinda Viljoen-Bloom. "Fungal Biotechnology: Fungal Amylases and Their Applications." In Reference Module in Life Sciences. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-12-809633-8.21082-0.
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MONTENECOURT, BLAND S., and DOUGLAS E. EVELEIGH. "Fungal Carbohydrases: Amylases and Cellulases." In Gene Manipulations in Fungi, 491–512. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-088640-1.50026-4.
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Khajuria, Robinka, and Shalini Singh. "Fungal Amylases for the Detergent Industry." In Microbes in Agriculture and Environmental Development, 153–64. CRC Press, 2020. http://dx.doi.org/10.1201/9781003057819-8.
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Nyika, Joan Mwihaki. "The Plastic Waste Menace and Approaches to Its Management Through Biodegradation." In Advances in Environmental Engineering and Green Technologies, 218–35. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-4921-6.ch010.
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In contemporary society, the production and use of plastics is growing due to their assorted applications. However, these tendencies result to production of plastic waste whose effects to the environment are destructive. This chapter explores the production tendencies of plastics and plastic-waste chronologically, discusses its negative environmental effects, and proposes the adoption of biodegradation as a management approach. A number of effects including death, retarded growth and development, emergence of cancers, and altered physiology are associated with ingestion of plastics in animals and humans. Water and air pollution is associated with unscientific disposal of plastic waste resulting to leaching and release of greenhouse gases. The use of microbes such as bacteria and fungi that have inherent enzymes such as lipases, esterases, hydrolases, and amylases is discussed as a sustainable solution to the plastic menace. The successful use of biodegradation must be coupled with scientific research to optimise the factors influencing the process.
Conference papers on the topic "Fungal amylase"
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Kuzikova, Irina, Irina Kuzikova, Vera Safronova, Vera Safronova, Nadezda Medvedeva, and Nadezda Medvedeva. "IMPACT OF NONYLPHENOL ON THE PHYSIOLOGICAL ACTIVITY OF FUNGI FROM THE COASTAL AREA OF THE GULF OF FINLAND." In Managing risks to coastal regions and communities in a changing world. Academus Publishing, 2017. http://dx.doi.org/10.21610/conferencearticle_58b431765a62a.
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Nonylphenol (NP) is the most abundant environmental estrogen listed as one of the priority hazardous substances in the Water Framework Directive (EC 2000) and the priority pollutant of Baltic Sea (HELCOM 2010). The present study aims to compare the effects of technical nonylphenol (tNP) on the cellulase, amylase and protease activity of the terrestrial fungal strains played a significant role in aquatic ecosystems due to their high adaptive capacity and a large range of functional activity. The study also attempts to understand the mechanisms behind the varying sensitivity of the terrestrial fungi to tNP. The fungal strains were isolated from the bottom sediments of the coastal area of the eastern part of the Gulf of Finland. The terrestrial fungi were identified based on their morphological characteristics and nucleotide sequence analysis of internal transcribed space region. One reason for significant differences in sensitivity to the toxicant studied among the fungi is the change in the fungal cell permeability, in particular in cell membrane permeability, induced by NP. Environmentally relevant concentrations of tNP cause significant changes in activity of hydrolytic enzymes in the terrestrial fungi Aspergillus tubingensis, Penicillium expansum, Penicillium glabrum, and Cadophora fastigiata involved in organic matter degradation in bottom sediments. There can be increasing or decreasing trend, depending on both the type of enzyme and the tNP concentration. The revealed changes may disrupt the destructive processes in bottom sediments, as well as succession and stability of microbial communities functioning in the aquatic environment. It was found that tNP contributes to the activation of proteolytic enzymes, considered as potential fungal virulence factors. This may lead to emergence fungal strains with enhanced virulence in aquatic microbiocenoses. The investigations of the physiological responses of terrestrial fungi under nonylphenol will be important for biochemical processes dynamics and their environmental consequences evaluation.
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Kuzikova, Irina, Irina Kuzikova, Vera Safronova, Vera Safronova, Nadezda Medvedeva, and Nadezda Medvedeva. "IMPACT OF NONYLPHENOL ON THE PHYSIOLOGICAL ACTIVITY OF FUNGI FROM THE COASTAL AREA OF THE GULF OF FINLAND." In Managing risks to coastal regions and communities in a changing world. Academus Publishing, 2017. http://dx.doi.org/10.31519/conferencearticle_5b1b93c5890b52.86067390.
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Nonylphenol (NP) is the most abundant environmental estrogen listed as one of the priority hazardous substances in the Water Framework Directive (EC 2000) and the priority pollutant of Baltic Sea (HELCOM 2010). The present study aims to compare the effects of technical nonylphenol (tNP) on the cellulase, amylase and protease activity of the terrestrial fungal strains played a significant role in aquatic ecosystems due to their high adaptive capacity and a large range of functional activity. The study also attempts to understand the mechanisms behind the varying sensitivity of the terrestrial fungi to tNP. The fungal strains were isolated from the bottom sediments of the coastal area of the eastern part of the Gulf of Finland. The terrestrial fungi were identified based on their morphological characteristics and nucleotide sequence analysis of internal transcribed space region. One reason for significant differences in sensitivity to the toxicant studied among the fungi is the change in the fungal cell permeability, in particular in cell membrane permeability, induced by NP. Environmentally relevant concentrations of tNP cause significant changes in activity of hydrolytic enzymes in the terrestrial fungi Aspergillus tubingensis, Penicillium expansum, Penicillium glabrum, and Cadophora fastigiata involved in organic matter degradation in bottom sediments. There can be increasing or decreasing trend, depending on both the type of enzyme and the tNP concentration. The revealed changes may disrupt the destructive processes in bottom sediments, as well as succession and stability of microbial communities functioning in the aquatic environment. It was found that tNP contributes to the activation of proteolytic enzymes, considered as potential fungal virulence factors. This may lead to emergence fungal strains with enhanced virulence in aquatic microbiocenoses. The investigations of the physiological responses of terrestrial fungi under nonylphenol will be important for biochemical processes dynamics and their environmental consequences evaluation.
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Hidayati, Wahyu, Ade Nur Padillah, Maharadingga, Ni Putu Ermi Hikmawanti, Rini Prastiwi, Ani Pratiwi, Lady Farahmayuni, Rezza Syahputra, and Muhammad Fahrul. "The Alpha-Amylase Inhibition Potential of Endophytic Fungi from Indonesian Bay Leaves (Eugenia polyantha WIGHT.)." In 1st Muhammadiyah International Conference on Health and Pharmaceutical Development. SCITEPRESS - Science and Technology Publications, 2018. http://dx.doi.org/10.5220/0008240201070111.
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Fifendy, Mades, Periadnadi, Gustina Indriati, Syovia Osnita, and Lara Annisa. "Isolation and Activity of Amylase Enzyme in Isolates of Fungi From Black Rice Lemang (Oryza sativa Siarang)." In International Conference on Biology, Sciences and Education (ICoBioSE 2019). Paris, France: Atlantis Press, 2020. http://dx.doi.org/10.2991/absr.k.200807.011.
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Rojas-Verde, G., M. M. Iracheta-Cárdenas, L. J. Galán-Wong, and K. Arévalo-Niño. "Production of amylases, CMCases, xylanases and ligninolytic enzymes by white-rot fungi in solid and liquid fermentation." In Proceedings of the III International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld2009). WORLD SCIENTIFIC, 2010. http://dx.doi.org/10.1142/9789814322119_0122.
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