01793nas a2200229 4500008004100000022001400041245009000055210006900145260009900214300001200313490000700325520097900332653001901311653002301330653001501353653001101368653001201379653001401391100001801405700002001423856012001443 2009 eng d a0964-830500aBiodegradation and phenol tolerance by recycled cells of candida tropicalis NCIM 35560 aBiodegradation and phenol tolerance by recycled cells of candida aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcJUN a539-5420 v633 a

Resting cells of Candida tropicalis NCIM 3556 rapidly degraded almost completely 2 g L(-1) phenol in 16h. In this study, we explored the possibility of further increasing the efficiency of the culture by repeatedly reusing the cell for biodegradation. The effect of continuous recycling of whole cells of C. tropicalis, for biodegradation of phenol indicated that though with each recycle of the cell there was steady decline in phenol biodegradation the conversion was appreciable for five recycle (similar to 70%) and reached half-life of 50% after eleven recycles. Inhibition due to substrate, recycling of cells and adaptation of residual cell were estimated and an equation derived; which indicated that the cell resilience to phenol increased with each cycle and at the end of eleven recycle adaptation was 68%. However, when the adapted cells were sub cultured and showed marginal increase <10% in biodegradation. (C) 2009 Elsevier Ltd. All rights reserved.

10aBiodegradation10aCandida tropicalis10aInhibition10aphenol10aRecycle10aTolerance1 aVarma, R., J.1 aGaikwad, B., G. uhttp://library.ncl.res.in/content/biodegradation-and-phenol-tolerance-recycled-cells-candida-tropicalis-ncim-3556-001666nas a2200229 4500008004100000022001400041245014200055210006900197260007300266300001400339490000700353520078800360653002101148653002201169653002501191653001501216653001501231653001801246100001901264700002501283856012801308 2011 eng d a0141-813000aJack bean alpha-mannosidase (Jb alpha-man): tolerance to alkali, chelating and reducing agents and energetics of catalysis and inhibition0 aJack bean alphamannosidase Jb alphaman tolerance to alkali chela aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcDEC a1066-10710 v493 a

Investigations of the catalytic and structural transitions of jack bean alpha-mannosidase (Jb alpha-man) are described in the present paper. The enzyme was maximally stable at pH 5.0; however, when incubated in the pH range of 11.0-12.0, showed 1.3 times higher activity and also stability for longer time. The free amino group at or near the active site was probably involved in the stability and activation mechanism. The active site is constituted by the association of two unidentical subunits connected by disulfide linkages. The metalloenzyme has Zn(2+) ions tightly bound and chelation reduces the thermal stability of the protein. Energetics of catalysis and thermodynamics of inhibition of the enzyme were also carried out. (C) 2011 Elsevier B.V. All rights reserved.

10aAlkali tolerance10aalpha-Mannosidase10abeta-Mercaptoethanol10aEnergetics10aInhibition10aMetalloenzyme1 aKumar, Avinash1 aGaikwad, Sushama, M. uhttp://library.ncl.res.in/content/jack-bean-alpha-mannosidase-jb-alpha-man-tolerance-alkali-chelating-and-reducing-agents-001921nas a2200265 4500008004100000022001400041245011800055210006900173260009500242300001200337490000800349520092800357653002401285653001201309653002301321653001501344653001901359653002301378100002901401700002601430700001901456700002401475700002601499856013001525 2013 eng d a0006-291X00aStructural modelling of substrate binding and inhibition in penicillin V acylase from pectobacterium atrosepticum0 aStructural modelling of substrate binding and inhibition in peni a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcAUG a538-5430 v4373 a

Penicillin V acylases (PVAs) and bile salt hydrolases (BSHs) have considerable sequence and structural similarity; however, they vary significantly in their substrate specificity. We have identified a PVA from a Gram-negative organism, Pectobacterium atrosepticum (PaPVA) that turned out to be a remote homolog of the PVAs and BSHs reported earlier. Even though the active site residues were conserved in PaPVA it showed high specificity towards penV and interestingly the penV acylase activity was inhibited by bile salts. Comparative modelling and docking studies were carried out to understand the structural differences of the binding site that confer this characteristic property. We show that PaPVA exhibits significant differences in structure, which are in contrast to those of known PVAs and such enzymes from Gram-negative bacteria require further investigation. (C) 2013 Elsevier Inc. All rights reserved.

10aBile salt hydrolase10adocking10aHomology modelling10aInhibition10aPectobacterium10aPenicillin acylase1 aAvinash, Vellore, Sunder1 aPanigrahi, Priyabrata1 aSuresh, C., G.1 aPundle, Archana, V.1 aRamasamy, Sureshkumar uhttp://library.ncl.res.in/content/structural-modelling-substrate-binding-and-inhibition-penicillin-v-acylase-pectobacterium-002577nas a2200217 4500008004100000022001400041245020200055210006900257260006900326300001000395490000800405520168600413653001902099653001502118653001802133653001302151653002402164653002302188100002902211856011902240 2015 eng d a1010-603000aInhibition effect of N,N-diglycidyl-4-glycidyloxy aniline on photosensitized cationic polymerization of formulations involving resorcinol diglycidyl ether and poly(propylene glycol)diglycidyl ether0 aInhibition effect of NNdiglycidyl4glycidyloxy aniline on photose aPO BOX 564, 1001 LAUSANNE, SWITZERLANDbELSEVIER SCIENCE SAcAPR a17-270 v3033 a

Cationic photopolymerization studies of poly(propylene glycol)diglycidyl ether with and without 25 wt% of resorcinol diglycidyl ether were carried out in presence of bis(4-methylphenyl)iodonium hexafluorophosphate as photoinitiator. Analyses were carried out using polychromatic radiation at different temperatures in a photo differential scanning calorimeter. The formulations showed an enhancement in the rate of polymerization on addition of resorcinol diglycidyl ether. The same formulations when subjected to photosensitized polymerization in presence of 1-chloro-4-propoxy-9H-thioxanthen-9-one, showed a reverse behavior in rate due to partial absorption of radiation by resorcinol diglycidyl ether. Studies carried out on by the addition of N,N-diglycidy1-4-glycidyloxy aniline as inhibitor on the photosensitized formulations showed higher scavenging activity by inhibitor. The addition of nitrogen containing epoxy monomer as inhibitor can lead to its possible crosslinking within the matrix on polymerization along with a decrease in rate of polymerization without compromising on the final observed conversion. This effect can occur readily for non vitrifying systems. Thus, this observation provides an insight into its possible usage in a rate controlled photopolymerizable epoxy formulations. The photopolymerization kinetics were found to depend on the nature of generation, propagation and scavenging of active centers which are heavily dependent on diffusional restrictions imparted by in situ viscosity of the system. The kinetic estimations as well as evaluation of autocatalytic kinetic model are investigated. (C) 2015 Elsevier B.V. All rights reserved.

10aGlycidyl ether10aInhibition10akinetic model10akinetics10aPhotopolymerization10aPhotosensitization1 aHarikrishna, Reghunathan uhttp://library.ncl.res.in/content/inhibition-effect-nn-diglycidyl-4-glycidyloxy-aniline-photosensitized-cationic-0