Substrate regulation on co-metabolic degradation of β-cypermethrin by Bacillus licheniformis B-1

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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Rhizobium radiobacter e Bacillus licheniformis: opportunistic peritonitis

10.26226/morressier.59a56f96d462b8028d895ec7 ◽

2017 ◽

Author(s):

Rute Carmo

Keyword(s):

Bacillus Licheniformis ◽

Rhizobium Radiobacter

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XYLANASE, AN ENVIRONMENTALLY FRIENDLY BLEACHING AGENT FOR PULP AND PAPER: Characterization And Stabilization Study Of Bacillus licheniformis I-5 CRUDE Xylanase

Jurnal Rekayasa Lingkungan ◽

10.29122/jrl.v7i3.1961 ◽

2018 ◽

Vol 7 (3) ◽

Author(s):

Budiasih Wahyuntari., dkk

Keyword(s):

Thermal Stability ◽

Bacillus Licheniformis ◽

Hot Spring ◽

Sodium Dodecyl ◽

Luria Broth ◽

Crude Enzyme ◽

Half Time ◽

Triton X100 ◽

Sds Page ◽

Xylanolytic Enzymes

Isolate I-5 was isolated from Ciseeng hot spring, West Java and was identified as Bacillus licheniformis I-5. The isolate produces extracellular xylanolytic enzymes on Oatspelt containing Luria broth agar medium. Optimal activity of the crude enzyme was Â observed at 50ÂºC and pH 7. The effect of sodium dodecyl sulphate, b-mercaptoethanol and Triton-X100 were observed. Incubating the crude enzyme in 1.5% SDS and 1.5% b-mercaptoethanol at 50oC for 90 minutes then adding Triton-X100 at final concentration of 3.5% for 45 minutes only reduced 5.75% of the initial enzyme activity. SDS/PAGE and zymogram analysis showed that at least two xylanolytic enzymes presence in the crude enzyme. The molecular weight of the enzyme was estimated about 127 and 20kD. The enzyme hydrolysed xylan into xylobiose, xylotriose and other longer xylooligosaccharides. Thermal stability of the crude enzyme was observed at 50, 60, and 70oC and pH 7 and 8. The results showed that the half time of the crude enzyme incubated at 50, 60, and 70oC pH 7 was 2 hours 55 minutes; 2 hours 33 minutes and 1 hour 15 minutes respectively. The half time at 50, 60 and 70oC, pH 8 was 2 hours 48 minutes; 1 hour 22 minutes and 1 hour 9 minutes respectively.keywords: Xilanase, Bacillus licheniformis I-5, thermal stability

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Probiotics in the diets of laying quails

Kormlenie sel'skohozjajstvennyh zhivotnyh i kormoproizvodstvo (Feeding of agricultural animals and feed production) ◽

10.33920/sel-05-2001-06 ◽

2020 ◽

pp. 60-66

Author(s):

O. Merzlyakova ◽

V. Rogachyev ◽

V. Chegodaev

Keyword(s):

Bacillus Subtilis ◽

Bacillus Licheniformis ◽

Egg Production ◽

Positive Impact ◽

Hematological Parameters ◽

Economic Effect ◽

Egg Laying ◽

Control Group ◽

Egg Mass ◽

The Cost

The efficiency of introducing probiotics based on strains of Bacillus subtilis, Bacillus licheniformis and their consortium in the amount of 150 g/t of feed into the diets of laying quails has been studied. The experiment lasting 182 days has been carried out on four groups of quails with 30 heads in each. The quails have been housed in the broiler battery in compliance with the required microclimate conditions. Quails of all groups have been received the main diet (compound feed) developed taking into account their age and physiological characteristics. The quails of the 1st, 2nd and 3rd experimental groups in addition to the main diet received probiotics (150 g/t compound feed) based on strains Bacillus subtilis, Bacillus licheniformis and their consortium, respectively. It has been found that feeding the laying quails of the consortium of strains Bacillus subtilis and Bacillus licheniformis had the most significant positive impact on their productive performance, it allowed to increase egg production by 7,81 %, egg laying intensity by 5,0 %, egg mass yield by 9,77 %, while reducing feed expenditures for 10 eggs by 13,35 %. The yield of hatching eggs has been increased by 7,03 %, hatchability of chickens from laid and fertilized eggs by 8,33 and 8,35 %, brooding waste decreased by 21,74 %. Hematological parameters of quails during the whole experiment were within the physiological norm. The economic effect calculated on the basis of data on the cost of compound feed, probiotics and the cost of sold eggs of quail laying was 14,56 % in the 3rd experimental group (in relation to the control group).

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Catalytic properties of the cloned amylase from Bacillus licheniformis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41642-0 ◽

1992 ◽

Vol 267 (31) ◽

pp. 22108-22114

Author(s):

I.C. Kim ◽

J.H. Cha ◽

J.R. Kim ◽

S.Y. Jang ◽

B.C. Seo ◽

...

Keyword(s):

Bacillus Licheniformis ◽

Catalytic Properties

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Deamidation and glycation of a Bacillus licheniformis α-amylase during industrial fermentation can improve detergent wash performance

Amylase ◽

10.1515/amylase-2021-0004 ◽

2021 ◽

Vol 5 (1) ◽

pp. 38-49

Author(s):

Connie Pontoppidan ◽

Svend G. Kaasgaard ◽

Carsten P. Sønksen ◽

Carsten Andersen ◽

Birte Svensson

Keyword(s):

Bacillus Licheniformis ◽

Mutational Analysis ◽

Peptide Mapping ◽

Substrate Binding ◽

Carbohydrate Binding ◽

Surface Binding ◽

Lysine Residues ◽

Tandem Mass Spectrometric ◽

Binding Cleft ◽

Household Detergents

Abstract The industrial thermostable Bacillus licheniformis α-amylase (BLA) has wide applications, including in household detergents, and efforts to improve its performance are continuously ongoing. BLA during the industrial production is deamidated and glycated resulting in multiple forms with different isoelectric points. Forty modified positions were identified by tandem mass spectrometric peptide mapping of BLA forms separated by isoelectric focusing. These modified 12 asparagine, 9 glutamine, 8 arginine and 11 lysine residues are mostly situated on the enzyme surface and several belong to regions involved in stability, activity and carbohydrate binding. Eight residues presumed to interact with starch at the active site and surface binding sites (SBSs) were subjected to mutational analysis. Five mutants mimicking deamidation (N→D, Q→E) at the substrate binding cleft showed moderate to no effect on thermostability and k cat and K M for maltoheptaose and amylose. Notably, the mutations improved laundry wash efficiency in detergents at pH 8.5 and 10.0. Replacing three reducing sugar reactive side chains (K→M, R→L) at a distant substrate binding region and two SBSs enhanced wash performance especially in liquid detergent at pH 8.5, slightly improved enzymatic activity and maintained thermostability. Wash performance was most improved (5-fold) for the N265D mutant near substrate binding subsite +3.

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Improving the Utility of a Dynorphin Peptide Analogue Using Mannosylated Glycoliposomes

International Journal of Molecular Sciences ◽

10.3390/ijms22157996 ◽

2021 ◽

Vol 22 (15) ◽

pp. 7996

Author(s):

Jordan D. Lewicky ◽

Nya L. Fraleigh ◽

Alexandrine L. Martel ◽

Thi M.-D. Nguyen ◽

Peter W. Schiller ◽

...

Keyword(s):

Targeted Delivery ◽

Delivery Systems ◽

Kappa Opioid Receptor ◽

Antagonist Activity ◽

Peptide Analogue ◽

Nanoparticle Delivery ◽

The Central Nervous System ◽

Metabolic Degradation ◽

Distribution Studies

Peptide therapeutics offer numerous advantages in the treatment of diseases and disorders of the central nervous system (CNS). However, they are not without limitations, especially in terms of their pharmacokinetics where their metabolic lability and low blood–brain barrier penetration hinder their application. Targeted nanoparticle delivery systems are being tapped for their ability to improve the delivery of therapeutics into the brain non-invasively. We have developed a family of mannosylated glycoliposome delivery systems for targeted drug delivery applications. Herein, we demonstrate via in vivo distribution studies the potential of these glycoliposomes to improve the utility of CNS active therapeutics using dynantin, a potent and selective dynorphin peptide analogue antagonist of the kappa opioid receptor (KOR). Glycoliposomal entrapment protected dynantin against known rapid metabolic degradation and ultimately improved brain levels of the peptide by approximately 3–3.5-fold. Moreover, we linked this improved brain delivery with improved KOR antagonist activity by way of an approximately 30–40% positive modulation of striatal dopamine levels 20 min after intranasal administration. Overall, the results clearly highlight the potential of our glycoliposomes as a targeted delivery system for therapeutic agents of the CNS.

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Screening for optimal protease producing Bacillus licheniformis strains with polymer-based controlled-release fed-batch microtiter plates

Microbial Cell Factories ◽

10.1186/s12934-021-01541-2 ◽

2021 ◽

Vol 20 (1) ◽

Author(s):

Tobias Habicher ◽

Tobias Klein ◽

Jacqueline Becker ◽

Andreas Daub ◽

Jochen Büchs

Keyword(s):

Controlled Release ◽

Bacillus Licheniformis ◽

Protease Activity ◽

Microtiter Plate ◽

Fed Batch ◽

Batch Mode ◽

Screening Process ◽

Microtiter Plates ◽

Batch Fermenter ◽

Production Conditions

Abstract Background Substrate-limited fed-batch conditions have the favorable effect of preventing overflow metabolism, catabolite repression, oxygen limitation or inhibition caused by elevated substrate or osmotic concentrations. Due to these favorable effects, fed-batch mode is predominantly used in industrial production processes. In contrast, screening processes are usually performed in microtiter plates operated in batch mode. This leads to a different physiological state of the production organism in early screening and can misguide the selection of potential production strains. To close the gap between screening and production conditions, new techniques to enable fed-batch mode in microtiter plates have been described. One of these systems is the ready-to-use and disposable polymer-based controlled-release fed-batch microtiter plate (fed-batch MTP). In this work, the fed-batch MTP was applied to establish a glucose-limited fed-batch screening procedure for industrially relevant protease producing Bacillus licheniformis strains. Results To achieve equal initial growth conditions for different clones with the fed-batch MTP, a two-step batch preculture procedure was developed. Based on this preculture procedure, the standard deviation of the protease activity of glucose-limited fed-batch main culture cultivations in the fed-batch MTP was ± 10%. The determination of the number of replicates revealed that a minimum of 6 parallel cultivations were necessary to identify clones with a statistically significant increased or decreased protease activity. The developed glucose-limited fed-batch screening procedure was applied to 13 industrially-relevant clones from two B. licheniformis strain lineages. It was found that 12 out of 13 clones (92%) were classified similarly as in a lab-scale fed-batch fermenter process operated under glucose-limited conditions. When the microtiter plate screening process was performed in batch mode, only 5 out of 13 clones (38%) were classified similarly as in the lab-scale fed-batch fermenter process. Conclusion The glucose-limited fed-batch screening process outperformed the usual batch screening process in terms of the predictability of the clone performance under glucose-limited fed-batch fermenter conditions. These results highlight that the implementation of glucose-limited fed-batch conditions already in microtiter plate scale is crucial to increase the precision of identifying improved protease producing B. licheniformis strains. Hence, the fed-batch MTP represents an efficient high-throughput screening tool that aims at closing the gap between screening and production conditions.

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