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Journal articles on the topic 'Enzymes Enzymes Bacteria'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Jordan, Albert, Eduard Torrents, Irma Sala, Ulf Hellman, Isidre Gibert, and Peter Reichard. "Ribonucleotide Reduction in Pseudomonas Species: Simultaneous Presence of Active Enzymes from Different Classes." Journal of Bacteriology 181, no. 13 (1999): 3974–80. http://dx.doi.org/10.1128/jb.181.13.3974-3980.1999.

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ABSTRACT Three separate classes of ribonucleotide reductases exist in nature. They differ widely in protein structure. Class I enzymes are found in aerobic bacteria and eukaryotes; class II enzymes are found in aerobic and anaerobic bacteria; class III enzymes are found in strict and facultative anaerobic bacteria. Usually, but not always, one organism contains only one or two (in facultative anaerobes) classes. Surprisingly, the genomic sequence of Pseudomonas aeruginosa contains sequences for each of the three classes. Here, we show by DNA hybridization that other species ofPseudomonas also

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Sharma, Neha, Shuchi Kaushik, and Rajesh Singh Tomar. "Isolation and Characterization of Extracellular Enzyme (Glutaminase and Urease) producing Bacteria isolated from Soil Samples of Different Regions of Gwalior, Madhya Pradesh, India." Research Journal of Biotechnology 16, no. 7 (2021): 122–29. http://dx.doi.org/10.25303/167rjbt12221.

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Microbial glutaminase and urease have demonstrated their benefits in various fields like medicinal, pharmaceutical and biotechnological industries. Keeping this viewpoint, the aim of the present study was the isolation and characterization of extracellular enzyme-producing bacteria from soil samples collected from different regions of Gwalior (M.P.). The isolated bacterial cultures were processed by serial dilution method and maintained on nutrient agar medium following standard microbiological laboratory practices for maintenance and preservation of bacteria. We screened out three enzyme prod

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Alrumman, Sulaiman, Yasser S. Mostafa Mostafa, Shekha Al-Qahtani, and Tarek H. Taha Taha. "Hydrolytic Enzyme Production by Thermophilic Bacteria Isolated from Saudi Hot Springs." Open Life Sciences 13, no. 1 (2018): 470–80. http://dx.doi.org/10.1515/biol-2018-0056.

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AbstractHydrolytic enzyme production by thermophilic bacteria isolated from hot springs in the southern region of Saudi Arabia was investigated. The physical and chemical properties of the hot springs prove to be an important environment for hydrolytic-enzyme-producing thermophilic bacteria. Eighty-four bacterial isolates were obtained from three hot springs: Al-Majardah, Al-Khubah and Al-Ardah. Screening of the isolates for enzyme production indicated that 78 isolates showed activity for one or more enzymes. Molecular identification and phylogenic analysis of selected promising isolates confi

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Sukmawati, Sukmawati, Melda Yunita, and Febrianti Rosalina. "Measurement of alpha-Amilase Enzymes in Bacillus subtilis Bacteria." Indonesian Journal of Biology Education 3, no. 2 (2021): 7. http://dx.doi.org/10.31002/ijobe.v3i2.3237.

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The bacterium Bacillus subtilis is able to produce amylase enzymes which are able to hydrolyze various types of starch sources into simple compounds such as maltose, glucose. Amylase converts carbohydrates which are polysaccharides into maltose. Amylase enzyme is a group of enzymes that are needed in the industrial field. The purpose of this study was to determine the level of the amylase enzyme produced by the bacterium Bacillus subtilis. The method used in this research is a quantitative method using an amylase enzyme measurement experiment. The results of this study are from two types of en

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Liu, Yuan, Ruichao Li, Xia Xiao, and Zhiqiang Wang. "Molecules that Inhibit Bacterial Resistance Enzymes." Molecules 24, no. 1 (2018): 43. http://dx.doi.org/10.3390/molecules24010043.

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Antibiotic resistance mediated by bacterial enzymes constitutes an unmet clinical challenge for public health, particularly for those currently used antibiotics that are recognized as “last-resort” defense against multidrug-resistant (MDR) bacteria. Inhibitors of resistance enzymes offer an alternative strategy to counter this threat. The combination of inhibitors and antibiotics could effectively prolong the lifespan of clinically relevant antibiotics and minimize the impact and emergence of resistance. In this review, we first provide a brief overview of antibiotic resistance mechanism by ba

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Chasanah, Ekowati, Mahrus Ali, and Miftahul Ilmi. "IDENTIFICATION AND PARTIAL CHARACTERIZATION OF CRUDE EXTRACELLULAR ENZYMES FROM BACTERIA ISOLATED FROM SHRIMP WASTE PROCESSING." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 7, no. 1 (2013): 11. http://dx.doi.org/10.15578/squalen.v7i1.11.

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Attention on chitin degrading enzymes has been growing since their ability to reduce the waste of shrimp/other crustaceans processing industries and converting them into value added products such as biologically active chitin and chitosan oligomer. Previous experiment found that KLU 11.16 isolate was one of the potential bacteria isolated from shrimp waste producing chitinolytic enzymes including chitosanases. A study on the identification of KLU 11.16 extracellularcrude enzyme was carried out by cultivating the bacteria on chitin medium. Due to the wide application of chitosanase, the charact

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Hallberg, Zachary F., Xin C. Wang, Todd A. Wright, et al. "Hybrid promiscuous (Hypr) GGDEF enzymes produce cyclic AMP-GMP (3′, 3′-cGAMP)." Proceedings of the National Academy of Sciences 113, no. 7 (2016): 1790–95. http://dx.doi.org/10.1073/pnas.1515287113.

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Over 30 years ago, GGDEF domain-containing enzymes were shown to be diguanylate cyclases that produce cyclic di-GMP (cdiG), a second messenger that modulates the key bacterial lifestyle transition from a motile to sessile biofilm-forming state. Since then, the ubiquity of genes encoding GGDEF proteins in bacterial genomes has established the dominance of cdiG signaling in bacteria. However, the observation that proteobacteria encode a large number of GGDEF proteins, nearing 1% of coding sequences in some cases, raises the question of why bacteria need so many GGDEF enzymes. In this study, we r

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Nababan, Monalisa, Ida Bagus Wayan Gunam, and I. Made Mahaputra Wijaya. "PRODUKSI ENZIM SELULASE KASAR DARI BAKTERI SELULOLITIK." JURNAL REKAYASA DAN MANAJEMEN AGROINDUSTRI 7, no. 2 (2019): 190. http://dx.doi.org/10.24843/jrma.2019.v07.i02.p03.

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The purpose of this research was to elucidate the potentials of cellulolytic bacteria isolates in producing crude cellulose enzymes and to determine the ability of exoglucanase enzymes and endoglucanase enzymes produced from selected cellulolytic bacteria isolates. Ten potential isolates from previous research were confirmed using 1% Carboxymethyl Cellulose (CMC) media with the addition of Congo red and four potential isolates were obtained which then crude cellulose production and enzyme activity tests were carried out using cellulose substrates such as Carboxymethyl Cellulose (CMC), and Filt

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Hutagalung, Truly M., A. Yelnetty, M. Tamasoleng, and J. H. W. Ponto. "PENGGUNAAN ENZIM RENNET DAN BAKTERI Lactobacillus plantarum YN 1.3 TERHADAP SIFAT SENSORIS KEJU." ZOOTEC 37, no. 2 (2017): 286. http://dx.doi.org/10.35792/zot.37.2.2017.16068.

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THE UTILIZING OF RENNET ENZYMES and Lactobacillus plantarum YN 1.3 BACTERIA ON SENSORY CHARACTERISTICS OF CHEESE. This research aims to determine the utilizing of rennet enzymes and Lactobacillus plantarum YN 1.3 bacteria on sensory characteristics of cheese. This experiment using a completely randomized design (CRD) with treatments level of rennet enzymes 10%, 8%, 6%, 4%, 2% and Lactobacillus plantarum YN 1.3 bacteria on 0%, 2%, 4%, 6%, 8% levels, which is each treatment repeated as much as 40 of replications (panelists) with hedonic method used. The result showed that the utilizing of rennet

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-, Shilpa, Mandheer Kaur, and Yogita Jadon. "Isolation and Screening of Pectinase Producing Bacteria from Soil Sample." CGC International Journal of Contemporary Technology and Research 3, no. 2 (2021): 166–70. http://dx.doi.org/10.46860/cgcijctr.2021.06.31.166.

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The vast majority of the industrial use of enzymes is covered from microorganisms. Microorganisms are favoured in industry because of their several advantages for example rapid growth, short life expectancy and simplicity in doing genetic alterations. Microbial enzymes are thus amply provided, very much standardized and promoted by many companies. Among various enzymes, Pectinases hold an exceptional place because of its different uses in various sectors like food, textile and biofuel industries.A total of 25% of total enzyme market is being shared by Pectinase alone.The current study was carr

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Khalifa, Moad, Ling Ling Few, and Wei Cun See Too. "ChoK-ing the Pathogenic Bacteria: Potential of Human Choline Kinase Inhibitors as Antimicrobial Agents." BioMed Research International 2020 (July 10, 2020): 1–14. http://dx.doi.org/10.1155/2020/1823485.

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Novel antimicrobial agents are crucial to combat antibiotic resistance in pathogenic bacteria. Choline kinase (ChoK) in bacteria catalyzes the synthesis of phosphorylcholine, which is subsequently incorporated into the cell wall or outer membrane. In certain species of bacteria, phosphorylcholine is also used to synthesize membrane phosphatidylcholine. Numerous human ChoK inhibitors (ChoKIs) have been synthesized and tested for anticancer properties. Inhibition of S. pneumoniae ChoK by human ChoKIs showed a promising effect by distorting the cell wall and retarded the growth of this pathogen.

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Susilowati, Prima Endang, Sapto Raharjo, Desi Kurniawati, Rahmawati Rahim, Sumarlin Sumarlin, and Ardiansyah Ardiansyah. "Produksi Xilanase dari Isolat Sumber Air Panas Sonai, Sulawesi Tenggara, menggunakan Limbah Pertanian." Jurnal Natur Indonesia 14, no. 3 (2013): 199. http://dx.doi.org/10.31258/jnat.14.3.199-204.

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Xylanase is the enzyme with prospec for hydrolysis hemicellulases. Many industry use xylanase thermostable. This processes require enzymes which are operationally stable at high temperature thus allowing e.g. easy mixing, better substrate solubility, high mass transfer rate, and lower risk of contamination. Thermophiles have often been proposed as sources of industrially relevant thermostable enzymes. Thermophilic bacteria, live at hot-springs, are can produced thermostable enzymes. In this work, we studied the bacteria strains isolated from water collected in the Sonai hot-springs of Southeas

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Octarya, Zona, Sumaryati Syukur, and Endang Purwati. "Purifikasi Parsial Enzim Ekstraseluler (Anoxybacillus sp.) yang Diisolasi dari Sumber Air Panas Bukit Kili Solok serta Aplikasinya untuk Menghidrolisis Limbah Berserat." Jurnal Natur Indonesia 15, no. 2 (2015): 106. http://dx.doi.org/10.31258/jnat.15.2.106-114.

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Termostable enzyme from thermophilic bacteria is very potential to improve technical enzyme in industry which used hightemperature. High water temperature exerts selection pressure on microbial species leading to specific flora that survivesand tolerates heat stress. The relative isolation and unique physical properties of Bukit Kili Ketek Hot Springs in Solok,West Sumatera may yield unique thermophiles. The generation of extracellular enzymatic bacterial is highly desirable forproduction of hydrolitic enzymes, which are useful in various industrial application and in animal feeds. This study,

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Ishak, Nadiah, Angzzas Sari Mohd Kassim, Ashuvila Mohd Aripin, Dayang Norulfairuz Abang Zaidel, and Muhd Hafeez Zainulabidin. "Identification and Expression of Ligninase Enzymes from Tropical Asia Wood Insect for Agro-Pulp Biodelignification: A Theoretical Framework." Applied Mechanics and Materials 773-774 (July 2015): 1380–83. http://dx.doi.org/10.4028/www.scientific.net/amm.773-774.1380.

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Current pulp-processing in pulp and paper based industries are inefficient in removing the lignin as this compound is recalcitrant towards degradation. Transitioning from conventional pulping process into bio-delignification through utilisation of ligninase enzymes is one of the alternatives to improve the ability to fully utilize all components of wood to produce high quality fibres. Extensive research efforts have been focused on increase the production of ligninase enzymes from white rot fungi as a whole organism for industrial applications. However, enzymes activity produced from fungi are

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15

Moon, Jae-Hyun, Sang-Jae Won, Chaw Ei Htwe Maung, et al. "The Role of Lysobacter antibioticus HS124 on the Control of Fall Webworm (Hyphantria cunea Drury) and Growth Promotion of Canadian Poplar (Populus canadensis Moench) at Saemangeum Reclaimed Land in Korea." Microorganisms 9, no. 8 (2021): 1580. http://dx.doi.org/10.3390/microorganisms9081580.

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Populus canadensis Moench forests established in Saemangeum-reclaimed land have been invaded by Hyphantria cunea Drury, causing defoliation and stunted growth. This study investigated the biocontrol potential of cuticle degrading chitinase and protease secreted by Lysobacter antibioticus HS124 against H. cunea larvae. In addition, L. antibioticus HS124 was examined for indole-3-acetic acid phytohormone production for plant growth promotion. To determine the larvicidal activity in the laboratory experiments, crude enzymes, bacteria culture, CY medium, and water (control) were sprayed on the lar

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Tropeano, Mauro, Susana Vázquez, Silvia Coria, et al. "Extracellular hydrolytic enzyme production by proteolytic bacteria from the Antarctic." Polish Polar Research 34, no. 3 (2013): 253–67. http://dx.doi.org/10.2478/popore-2013-0014.

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AbstractCold−adapted marine bacteria producing extracellular hydrolytic enzymes are important for their industrial application and play a key role in degradation of particulate organic matter in their natural environment. In this work, members of a previously−obtained protease−producing bacterial collection isolated from different marine sources from Potter Cove (King George Island, South Shetlands) were taxonomically identified and screened for their ability to produce other economically relevant enzymes. Eighty−eight proteolytic bacterial isolates were grouped into 25 phylotypes based on the

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Jendresen, Christian Bille, Steen Gustav Stahlhut, Mingji Li, et al. "Highly Active and Specific Tyrosine Ammonia-Lyases from Diverse Origins Enable Enhanced Production of Aromatic Compounds in Bacteria and Saccharomyces cerevisiae." Applied and Environmental Microbiology 81, no. 13 (2015): 4458–76. http://dx.doi.org/10.1128/aem.00405-15.

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ABSTRACTPhenylalanine and tyrosine ammonia-lyases form cinnamic acid andp-coumaric acid, which are precursors of a wide range of aromatic compounds of biotechnological interest. Lack of highly active and specific tyrosine ammonia-lyases has previously been a limitation in metabolic engineering approaches. We therefore identified 22 sequencesin silicousing synteny information and aiming for sequence divergence. We performed a comparativein vivostudy, expressing the genes intracellularly in bacteria and yeast. When produced heterologously, some enzymes resulted in significantly higher production

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Littlechild, Jennifer A. "Thermophilic archaeal enzymes and applications in biocatalysis." Biochemical Society Transactions 39, no. 1 (2011): 155–58. http://dx.doi.org/10.1042/bst0390155.

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Thermophilic enzymes have advantages for their use in commercial applications and particularly for the production of chiral compounds to produce optically pure pharmaceuticals. They can be used as biocatalysts in the application of ‘green chemistry’. The thermophilic archaea contain enzymes that have already been used in commercial applications such as the L-aminoacylase from Thermococcus litoralis for the resolution of amino acids and amino acid analogues. This enzyme differs from bacterial L-aminoacylases and has similarities to carboxypeptidases from other archaeal species. An amidase/γ-lac

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Strunk, Robert J., Katrina M. Piemonte, Natasha M. Petersen, et al. "Structure determination of BA0150, a putative polysaccharide deacetylase fromBacillus anthracis." Acta Crystallographica Section F Structural Biology Communications 70, no. 2 (2014): 156–59. http://dx.doi.org/10.1107/s2053230x13034262.

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Polysaccharide deacetylases are bacterial enzymes that catalyze the deacetylation of acetylated sugars on the membranes of Gram-positive bacteria, allowing them to be unrecognized by host immune systems. Inhibition of these enzymes would disrupt such pathogenic defensive mechanisms and therefore offers a promising route for the development of novel antibiotic therapeutics. Here, the first X-ray crystal structure of BA0150, a putative polysaccharide deacetylase fromBacillus anthracis, is reported to 2.0 Å resolution. The overall structure maintains the conserved (α/β)8fold that is characteristi

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KHALILA, RUHUL, Lenni Fitri, and SUHARTONO SUHARTONO. "Isolation and Characterization of Thermophilic Bacteria as Cellulolytic Enzyme Producer from the Hot Spring of Ie Seuum Aceh Besar, Indonesia." Microbiology Indonesia 14, no. 1 (2020): 4. http://dx.doi.org/10.5454/mi.14.1.4.

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Cellulase enzymes can be isolated from thermophile bacteria obtained from the hot spring Ie Seuum, Aceh Besar. This research aimed to recover and characterize the isolates morphologically and biochemically followed by determination of the thermophile bacterial isolates potential as cellulolytic enzyme producers,. The sampling method in this research was conducted by a purposive sampling at temperature of 70 oC, 60 oC and 50 oC. Isolation of thermophilic bacteria was carried out on nutrient agar (NA) media. There were four isolates of thermophilic bacteria isolated recovered at 70 oC, five isol

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Yamasaki, Takashi, Yuka Miyazaki, and Yuto Kamei. "Isolation of bacteria that decompose major polysaccharides in the cell wall of the marine red alga Porphyra yezoensis and their application for protoplast production." Canadian Journal of Microbiology 44, no. 8 (1998): 789–94. http://dx.doi.org/10.1139/w98-070.

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We attempted to screen for bacteria that could decompose major polysaccharides in the cell wall of the marine red alga Porphyra yezoensis from Porphyra-culturing farms to enable simple and high-yield preparation of protoplasts with the crude enzyme from a single bacterial origin. A total of 275 positive bacterial strains were isolated by enrichment culture supplemented with Porphyra powder or xylan. Nine strains were capable of producing protoplasts from Porphyra thalli in a 10-fold concentrated culture broth. These strains were identified as two Flavobacterium spp., one Alteromonas sp., four

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Moroz, Olga V., Elena Blagova, Andrey A. Lebedev, et al. "The structure of a calcium-dependent phosphoinositide-specific phospholipase C fromPseudomonassp. 62186, the first from a Gram-negative bacterium." Acta Crystallographica Section D Structural Biology 73, no. 1 (2017): 32–44. http://dx.doi.org/10.1107/s2059798316019616.

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Bacterial phosphoinositide-specific phospholipases C (PI-PLCs) are the smallest members of the PI-PLC family, which includes much larger mammalian enzymes responsible for signal transduction as well as enzymes from protozoan parasites, yeast and plants. Eukaryotic PI-PLCs have calcium in the active site, but this is absent in the known structures of Gram-positive bacteria, where its role is instead played by arginine. In addition to their use in a number of industrial applications, the bacterial enzymes attract special interest because they can serve as convenient models of the catalytic domai

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Barney, Brett M., Bradley D. Wahlen, EmmaLee Garner, Jiashi Wei, and Lance C. Seefeldt. "Differences in Substrate Specificities of Five Bacterial Wax Ester Synthases." Applied and Environmental Microbiology 78, no. 16 (2012): 5734–45. http://dx.doi.org/10.1128/aem.00534-12.

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ABSTRACTWax esters are produced in certain bacteria as a potential carbon and energy storage compound. The final enzyme in the biosynthetic pathway responsible for wax ester production is the bifunctional wax ester synthase/acyl-coenzyme A (acyl-CoA):diacylglycerol acyltransferase (WS/DGAT), which utilizes a range of fatty alcohols and fatty acyl-CoAs to synthesize the corresponding wax ester. We report here the isolation and substrate range characterization for five WS/DGAT enzymes from four different bacteria:Marinobacter aquaeoleiVT8,Acinetobacter baylyi,Rhodococcus jostiiRHA1, andPsychroba

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Mitchell, Spencer J., Deeptak Verma, Karl E. Griswold, and Chris Bailey-Kellogg. "Building blocks and blueprints for bacterial autolysins." PLOS Computational Biology 17, no. 4 (2021): e1008889. http://dx.doi.org/10.1371/journal.pcbi.1008889.

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Bacteria utilize a wide variety of endogenous cell wall hydrolases, or autolysins, to remodel their cell walls during processes including cell division, biofilm formation, and programmed death. We here systematically investigate the composition of these enzymes in order to gain insights into their associated biological processes, potential ways to disrupt them via chemotherapeutics, and strategies by which they might be leveraged as recombinant antibacterial biotherapies. To do so, we developed LEDGOs (lytic enzyme domains grouped by organism), a pipeline to create and analyze databases of aut

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Remijawa, Ermi Sustika, Anggreni D. N. Rupidara, James Ngginak, and Ocky Karna Radjasa. "ISOLASI DAN SELEKSI BAKTERI PENGHASIL ENZIM EKSTRASELULER PADA TANAH MANGROVE DI PANTAI NOELBAKI." JURNAL ENGGANO 5, no. 2 (2020): 164–80. http://dx.doi.org/10.31186/jenggano.5.2.164-180.

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Bakteri yang hidup pada tanah mangrove bersifat halofilik yaitu mampu hidup pada lingkungan dengan kondisi kadar garam yang tinggi. Bakteri yang hidup pada zona yang ekstrim memerlukan protein yang tinggi untuk mempertahankan hidup dan dapat melakukan metabolisme, salah satunya dengan membentuk enzim terutama enzim ekstra seluler (enzim amilase, protease, selulase dan lipase). Tujuannya yaitu untuk mengisolasi dan menyeleksi bakteri penghasil enzim ekstraseluler. Metode yang digunakan adalah survey dan eksperimental terhadap isolasi bakteri dari tanah mangrove yang dikarakterisasi berdasarkan

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Slamovits, Claudio H., and Patrick J. Keeling. "Pyruvate-Phosphate Dikinase of Oxymonads and Parabasalia and the Evolution of Pyrophosphate-Dependent Glycolysis in Anaerobic Eukaryotes." Eukaryotic Cell 5, no. 1 (2006): 148–54. http://dx.doi.org/10.1128/ec.5.1.148-154.2006.

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ABSTRACT In pyrophosphate-dependent glycolysis, the ATP/ADP-dependent enzymes phosphofructokinase (PFK) and pyruvate kinase are replaced by the pyrophosphate-dependent PFK and pyruvate phosphate dikinase (PPDK), respectively. This variant of glycolysis is widespread among bacteria, but it also occurs in a few parasitic anaerobic eukaryotes such as Giardia and Entamoeba spp. We sequenced two genes for PPDK from the amitochondriate oxymonad Streblomastix strix and found evidence for PPDK in Trichomonas vaginalis and other parabasalia, where this enzyme was thought to be absent. The Streblomastix

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Oluoch, Kevin Raymond, Patrick Wafula Okanya, Rajni Hatti-Kaul, Bo Mattiasson, and Francis Jakim Mulaa. "Protease-, Pectinase- and Amylase- Producing Bacteria from a Kenyan Soda Lake." Open Biotechnology Journal 12, no. 1 (2018): 33–45. http://dx.doi.org/10.2174/1874070701812010033.

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Background:Alkaline enzymes are stable biocatalysts with potential applications in industrial technologies that offer high quality products.Objective:The growing demand for alkaline enzymes in industry has enhanced the search for microorganisms that produce these enzymes.Methods:Eighteen bacterial isolates from Lake Bogoria, Kenya, were screened for alkaline proteases, pectinases and amylases; characterized and subjected to quantitative analysis of the enzymes they produced.Results:The screening analysis ranked 14, 16 and 18 of the bacterial isolates as potent producers of alkaline proteases,

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Rori, Chindy Achika, Febby Ester Fany Kandou, and Agustina Monalisa Tangapo. "Aktivitas Enzim Ekstraseluler dari Bakteri Endofit Tumbuhan Mangrove Avicennia marina." JURNAL BIOS LOGOS 11, no. 2 (2020): 48. http://dx.doi.org/10.35799/jbl.11.2.2020.28338.

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ABSTRAKBakteri endofit merupakan salah satu sumber penghasil senyawa ekstraseluler yaitu enzim. Enzim dari bakteri endofit lebih menguntungkan dan produksinya lebih cepat. Penelitian ini bertujuan untuk menganalisis kemampuan aktivitas enzim ekstraseluler dari bakteri endofit tumbuhan mangrove Avicennia marina. Metode penelitian yang digunakan yaitu eksploratif eksperimental, melakukan isolasi bakteri dari tumbuhan mangrove A. marina dan selanjutnya dilakukan uji potensi aktivitas enzim ekstraseluler dari isolat bakteri endofit. Hasil isolasi memperoleh tujuh isolat bakteri endofit dari tumbuh

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van Hijum, Sacha A. F. T., Slavko Kralj, Lukasz K. Ozimek, Lubbert Dijkhuizen, and Ineke G. H. van Geel-Schutten. "Structure-Function Relationships of Glucansucrase and Fructansucrase Enzymes from Lactic Acid Bacteria." Microbiology and Molecular Biology Reviews 70, no. 1 (2006): 157–76. http://dx.doi.org/10.1128/mmbr.70.1.157-176.2006.

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SUMMARY Lactic acid bacteria (LAB) employ sucrase-type enzymes to convert sucrose into homopolysaccharides consisting of either glucosyl units (glucans) or fructosyl units (fructans). The enzymes involved are labeled glucansucrases (GS) and fructansucrases (FS), respectively. The available molecular, biochemical, and structural information on sucrase genes and enzymes from various LAB and their fructan and α-glucan products is reviewed. The GS and FS enzymes are both glycoside hydrolase enzymes that act on the same substrate (sucrose) and catalyze (retaining) transglycosylation reactions that

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Hamsina, Hamsina, M. Tang, and Erni Indrawati Ruslan Hasani. "Activity Test, Selectivity, Stability of Chitinase on Amobil Chitosan Membranes." International Journal of Multicultural and Multireligious Understanding 8, no. 7 (2021): 453. http://dx.doi.org/10.18415/ijmmu.v8i7.2750.

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The use of enzymes for industrial functions needs enzymes that are stable, selective and might be used repeatedly. The aim of the study was to determine the chitinase enzyme's function, selectivity, and stability in amobil chitosan membranes. The research method consisted of stages: production of the chitinase enzyme which included the manufacture of chitin colloidal substrate, rejuvenation of thermophilic bacteria, preparation of the inoculum and determining the optimum time of production, fractionation of ammonium sulfate, chitinase enzyme immobilization technique and activity, stability and

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Gedela, Ravi, Naga Sai Babu Makke, and Dinesh Karra. "A Metagenomics Analysis on B-Carotene Synthesis in Neurospora Crassa." International Journal of Applied Sciences and Biotechnology 3, no. 3 (2015): 490–503. http://dx.doi.org/10.3126/ijasbt.v3i3.13306.

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We have studied insilico on evolutionary uniqueness of phytoene synthase, which is one of the regulatory enzymes of ?-carotene synthesis in Neurospora crassa. This study reveals multiple sequence alignments showed high sequences with similarity within a species of bacteria, fungi and higher plants. This results designate interestingly between species of bacteria-fungi, fungi-plant, and among the species of bacteria-fungi-plant, showed tremendously less sequence with similarity, except bacteria-plant (high sequence with similarity) respectively. In Phylogenetics tree analysis showed within spec

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Krivobok, Serge, Sylvain Kuony, Christine Meyer, Mathilde Louwagie, John C. Willison, and Yves Jouanneau. "Identification of Pyrene-Induced Proteins in Mycobacterium sp. Strain 6PY1: Evidence for Two Ring-Hydroxylating Dioxygenases." Journal of Bacteriology 185, no. 13 (2003): 3828–41. http://dx.doi.org/10.1128/jb.185.13.3828-3841.2003.

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ABSTRACT In this study, the enzymes involved in polycyclic aromatic hydrocarbon (PAH) degradation were investigated in the pyrene-degrading Mycobacterium sp. strain 6PY1. [14C]pyrene mineralization experiments showed that bacteria grown with either pyrene or phenanthrene produced high levels of pyrene-catabolic activity but that acetate-grown cells had no activity. As a means of identifying specific catabolic enzymes, protein extracts from bacteria grown on pyrene or on other carbon sources were analyzed by two-dimensional gel electrophoresis. Pyrene-induced proteins were tentatively identifie

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Corral, Juan Carlos Coronado, Sergio de los Santos Villalobos, Lilia Arely Prado Barrgàn, et al. "Isolation of Moderately Halophilic Bacteria in Saline Environments of Sonora State Searching for Proteolytic Hydrolases." Open Agriculture 3, no. 1 (2018): 207–13. http://dx.doi.org/10.1515/opag-2018-0021.

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Abstract The aim of the study was to isolate moderately halophilic bacteria that produce proteolytic enzymes with industrial biotechnological value. Screening of halophiles from various saline habitats, led to the isolation of 210 moderately halophilic bacteria producing industrially important hydrolases; such as proteases, which are enzymes that hydrolyze the peptide bonds of proteins, represent one of the three groups of industrial enzymes. The present study of halophilic bacteria, producing proteases and isolated from different saline soils of Sonora State, was divided in two parts: the fir

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Sunna, A., and G. Antranikian. "Xylanolytic Enzymes from Fungi and Bacteria." Critical Reviews in Biotechnology 17, no. 1 (1997): 39–67. http://dx.doi.org/10.3109/07388559709146606.

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Spirig, Thomas, Ethan M. Weiner, and Robert T. Clubb. "Sortase enzymes in Gram-positive bacteria." Molecular Microbiology 82, no. 5 (2011): 1044–59. http://dx.doi.org/10.1111/j.1365-2958.2011.07887.x.

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Law, Jean, and Alfred Haandrikman. "Proteolytic enzymes of lactic acid bacteria." International Dairy Journal 7, no. 1 (1997): 1–11. http://dx.doi.org/10.1016/0958-6946(95)00073-9.

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THYAGARAJA, NAGAPPA, and AKIYOSHI HOSONO. "Antimutagenicity of Lactic Acid Bacteria from “Idly” Against Food-Related Mutagens." Journal of Food Protection 56, no. 12 (1993): 1061–66. http://dx.doi.org/10.4315/0362-028x-56.12.1061.

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Lactic acid bacteria from “Idly”, a traditional cereal pulse product of southern India, were evaluated for antimutagenic properties. Effect of their presence in Salmonella mutagenicity assay with foodborne mutagens like spice extracts, amino acid pyrolysates, and aflatoxins was examined. Variation of antimutagenic potential at different growth stages of these lactic acid bacteria was examined in time-course studies. The enzyme profile was examined to determine any possible relationship between antimutagenicity and enzymes in these lactic acid bacteria. Most of the lactic acid bacteria tested w

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Dong, Y., H. D. Bae, T. A. McAllister, G. W. Mathison та K. J. Cheng. "Effects of exogenous fibrolytic enzymes, α-bromoethanesulfonate and monensin on fermentation in a rumen simulation (RUSITEC) system". Canadian Journal of Animal Science 79, № 4 (1999): 491–98. http://dx.doi.org/10.4141/a99-024.

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The effects of exogenous fibrolytic enzymes, α-bromoethanesulfonate (BES) and monensin on fermentation and digestibility of grass hay were examined using two rumen simulation technique (RUSITEC) devices, each equipped with eight 820-mL fermenters with a liquid dilution rate of 0.73 d−1. Grass hay (10 g d−1) was fed either untreated or pre-treated with 0.2 g each of cellulase and xylanase, and in combination with no chemical or daily dosing of 20.5 µmol monensin, 20.5 µmol BES or 41 µmol BES. Pretreatment of hay with the fibrolytic enzymes increased (P < 0.05) organic matter (OM), cellulose

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Denta Putri, Lupita, Hasnah Natsir, and Seniwati Dali. "Thermophilic Xylanase Production Rom Isolates of Macula’ Hot Springs Bacteria Using Corn Cobs Waste Media." Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta) 10, no. 2 (2019): 25. http://dx.doi.org/10.20956/ica.v10i2.6652.

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Xylanases is an extracellular enzyme that has prospects as enzymes that hydrolyze hemicellulose (xylan). In this study, carried out isolatied of bacteria from the hot springs Makula', Tana Toraja and determine the optimum conditions in producing the xylanase enzyme. The steps being taken are the rejuvenation of bacteria, the manufacture medium inoculum and the production medium, the measurement OD (Optical Density) measurements of protein and testing activities xylanase. The results obtained showed that the production time for B. stearothermophilus SL3A is in the 48 hours with a value of 0.123

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Ziesche, Lisa, Jan Rinkel, Jeroen S. Dickschat, and Stefan Schulz. "Acyl-group specificity of AHL synthases involved in quorum-sensing in Roseobacter group bacteria." Beilstein Journal of Organic Chemistry 14 (June 5, 2018): 1309–16. http://dx.doi.org/10.3762/bjoc.14.112.

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N-Acylhomoserine lactones (AHLs) are important bacterial messengers, mediating different bacterial traits by quorum sensing in a cell-density dependent manner. AHLs are also produced by many bacteria of the marine Roseobacter group, which constitutes a large group within the marine microbiome. Often, specific mixtures of AHLs differing in chain length and oxidation status are produced by bacteria, but how the biosynthetic enzymes, LuxI homologs, are selecting the correct acyl precursors is largely unknown. We have analyzed the AHL production in Dinoroseobacter shibae and three Phaeobacter inhi

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Khan, Fazlurrahman, Sandra Folarin Oloketuyi, and Young-Mog Kim. "Diversity of Bacteria and Bacterial Products as Antibiofilm and Antiquorum Sensing Drugs Against Pathogenic Bacteria." Current Drug Targets 20, no. 11 (2019): 1156–79. http://dx.doi.org/10.2174/1389450120666190423161249.

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The increase in antibiotic resistance of pathogenic bacteria has led to the development of new therapeutic approaches to inhibit biofilm formation as well as interfere quorum sensing (QS) signaling systems. The QS system is a phenomenon in which pathogenic bacteria produce signaling molecules that are involved in cell to cell communication, production of virulence factors, biofilm maturation, and several other functions. In the natural environment, several non-pathogenic bacteria are present as mixed population along with pathogenic bacteria and they control the behavior of microbial community

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Kaplan, Jeffrey B. "Therapeutic Potential of Biofilm-Dispersing Enzymes." International Journal of Artificial Organs 32, no. 9 (2009): 545–54. http://dx.doi.org/10.1177/039139880903200903.

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Surface-attached colonies of bacteria known as biofilms play a major role in the pathogenesis of medical device infections. Biofilm colonies are notorious for their resistance to antibiotics and host defenses, which makes most device infections difficult or impossible to eradicate. Bacterial cells in a biofilm are held together by an extracellular polymeric matrix that is synthesized by the bacteria themselves. Enzymes that degrade biofilm matrix polymers have been shown to inhibit bio film formation, detach established bio film colonies, and render biofilm cells sensitive to killing by antimi

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Mawati, Sefi Desfeni, Esti Harpen, and Hilma Putri Fidyandini. "SKRINING BAKTERI TERMOFILIK POTENSIAL AMILOLITIK DARI SUMBER AIR PANAS WAY BELERANG KALIANDA LAMPUNG SELATAN." Journal of Aquatropica Asia 6, no. 1 (2021): 1–7. http://dx.doi.org/10.33019/aquatropica.v6i1.2458.

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Thermophilic bacteria that produced amylase and protease have been isolated from Way Belerang hot spring, Kalianda, South Lampung. This research aims to screen and identify thermophilic bacteria that have the potential to produce thermostable amylase and protease enzymes.The research procedures included sampling, isolation of enzyme-producing thermophilic bacteria, a series of phenotypic and biochemical tests, and molecular identification by 16s rRNA. This study used 2 treatments, namely incubation temperature 37 and 50 ºC with 3 repetitions. The results showed that the optimum temperature for

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Berlemont, Renaud, and Adam C. Martiny. "Genomic Potential for Polysaccharide Deconstruction in Bacteria." Applied and Environmental Microbiology 81, no. 4 (2014): 1513–19. http://dx.doi.org/10.1128/aem.03718-14.

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ABSTRACTGlycoside hydrolases are important enzymes that support bacterial growth by enabling the degradation of polysaccharides (e.g., starch, cellulose, xylan, and chitin) in the environment. Presently, little is known about the overall phylogenetic distribution of the genomic potential to degrade these polysaccharides in bacteria. However, knowing the phylogenetic breadth of these traits may help us predict the overall polysaccharide processing in environmental microbial communities. In order to address this, we identified and analyzed the distribution of 392,166 enzyme genes derived from 53

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Nyachoti, Charles Martin. "370 Awardee Talk: Role of feed enzymes in gut health and function." Journal of Animal Science 98, Supplement_4 (2020): 111–12. http://dx.doi.org/10.1093/jas/skaa278.205.

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Abstract Exogenous enzymes are routinely added to diets for non-ruminant animals, mainly to help enhance energy and nutrient utilization, thus contributing to efficient and sustainable production systems. Also, feed enzymes allow for effective utilization of non-traditional feedstuffs (e.g. co-products) in non-ruminant diets, with potential to mitigate feed cost. In addition to increased nutrient utilization, however, feed enzymes, through their impact on the gastrointestinal environment and microbial composition, can have a profound effect on indices of gut health and function. These effects

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Flores-Díaz, Marietta, Laura Monturiol-Gross, Claire Naylor, Alberto Alape-Girón, and Antje Flieger. "Bacterial Sphingomyelinases and Phospholipases as Virulence Factors." Microbiology and Molecular Biology Reviews 80, no. 3 (2016): 597–628. http://dx.doi.org/10.1128/mmbr.00082-15.

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SUMMARYBacterial sphingomyelinases and phospholipases are a heterogeneous group of esterases which are usually surface associated or secreted by a wide variety of Gram-positive and Gram-negative bacteria. These enzymes hydrolyze sphingomyelin and glycerophospholipids, respectively, generating products identical to the ones produced by eukaryotic enzymes which play crucial roles in distinct physiological processes, including membrane dynamics, cellular signaling, migration, growth, and death. Several bacterial sphingomyelinases and phospholipases are essential for virulence of extracellular, fa

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Klemme, J. H. "Photoproduction of Hydrogen by Purple Bacteria: A Critical Evaluation of the Rate Limiting Enzymatic Steps." Zeitschrift für Naturforschung C 48, no. 5-6 (1993): 482–87. http://dx.doi.org/10.1515/znc-1993-5-613.

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Abstract The enzymatic mechanisms and energetics of nitrogenase-catalyzed photoproduction of hydrogen from organic C-compounds by purple bacteria are discussed in respect to the question of which of the following three enzymes or enzyme systems are rate limiting for H2-production: (a) the nitrogenase-complex; (b) the enzymes and electron transport proteins involved in hydrogen transfer from the organic substrate(s) to nitrogenase; and (c) the system of photosynthetic ATP-regeneration. Calculations of maximum in vivo rates of photosynthetic ATPregeneration (gATP-values derived from growth rates

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Schreiner, Mark E., Diana Fiur, Jiří Holátko, Miroslav Pátek, and Bernhard J. Eikmanns. "E1 Enzyme of the Pyruvate Dehydrogenase Complex in Corynebacterium glutamicum: Molecular Analysis of the Gene and Phylogenetic Aspects." Journal of Bacteriology 187, no. 17 (2005): 6005–18. http://dx.doi.org/10.1128/jb.187.17.6005-6018.2005.

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ABSTRACT The E1p enzyme is an essential part of the pyruvate dehydrogenase complex (PDHC) and catalyzes the oxidative decarboxylation of pyruvate with concomitant acetylation of the E2p enzyme within the complex. We analyzed the Corynebacterium glutamicum aceE gene, encoding the E1p enzyme, and constructed and characterized an E1p-deficient mutant. Sequence analysis of the C. glutamicum aceE gene and adjacent regions revealed that aceE is not flanked by genes encoding other enzymes of the PDHC. Transcriptional analysis revealed that aceE from C. glutamicum is monocistronic and that its transcr

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Koga, Yosuke, and Hiroyuki Morii. "Biosynthesis of Ether-Type Polar Lipids in Archaea and Evolutionary Considerations." Microbiology and Molecular Biology Reviews 71, no. 1 (2007): 97–120. http://dx.doi.org/10.1128/mmbr.00033-06.

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SUMMARY This review deals with the in vitro biosynthesis of the characteristics of polar lipids in archaea along with preceding in vivo studies. Isoprenoid chains are synthesized through the classical mevalonate pathway, as in eucarya, with minor modifications in some archaeal species. Most enzymes involved in the pathway have been identified enzymatically and/or genomically. Three of the relevant enzymes are found in enzyme families different from the known enzymes. The order of reactions in the phospholipid synthesis pathway (glycerophosphate backbone formation, linking of glycerophosphate w

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Frébortová, Jitka, and Ivo Frébort. "Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria." Microorganisms 9, no. 6 (2021): 1314. http://dx.doi.org/10.3390/microorganisms9061314.

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It has been known for quite some time that cytokinins, hormones typical of plants, are also produced and metabolized in bacteria. Most bacteria can only form the tRNA-bound cytokinins, but there are examples of plant-associated bacteria, both pathogenic and beneficial, that actively synthesize cytokinins to interact with their host. Similar to plants, bacteria produce diverse cytokinin metabolites, employing corresponding metabolic pathways. The identification of genes encoding the enzymes involved in cytokinin biosynthesis and metabolism facilitated their detailed characterization based on bo

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