02327nas a2200253   4500008004100000022001400041245013200055210006900187260009900256300001200355490000700367520135500374653002501729653002601754653002501780653001701805653002701822653002601849100001601875700002101891700001901912700002001931856012201951       2008                        eng d  a1359-511300aCharacterization of smallest active monomeric penicillin V acylase from new source: a yeast, rhodotorula aurantiaca (NCIM 3425)0 aCharacterization of smallest active monomeric penicillin V acyla  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcSEP  a961-9670 v433 a<p>An intracellular monomeric penicillin V acylase (PVA) of 36,000 Da exhibiting pI of 4.19, purified from newly identified yeast source, Rhodotorula aurantiaca (NCIM 3425). The enzyme was purified by hydrophobic interaction chromatography. The enzyme showed optimal activity at 45 degrees C and retained 80% activity after incubation at 45 degrees C and pH 5.5 for I h. The enzyme showed maximum activity at pH 5.5 and was very stable between pH 5.5-6.5 with optimum stability at pH 6.0. It exhibited 50% of its original activity after 30 min incubation at 60 degrees C. Enzyme hydrolyzed substrates with benzyl side chain but preferred penicillin V as primary substrate. N-terminally located serine supports the fact that it belongs to Ntn (N-terminal nucleophile)-hydrolase superfamily. The initial ten amino acid residues of R. aurantiaca PVA were identical to the initial sequence of NADH dehydrogenase (EC 1.6.99.3): however the enzyme lacks dehydrogenase activity. EGTA, EDTA, hexane and ethyl acetate stabilized the activity where as small chain alcohols inhibited it. 1,4-Dioxane, THF (tetrahydrofurane), phenol and benzyl alcohol severely inhibited enzyme activity while BME and DTT increased it. Tween 80 and Tween 20 highly enhanced the activity where as SIDS and Triton X-100 inhibited it. (C) 2008 Elsevier Ltd. All rights reserved.</p>10aIntracellular enzyme10aN-terminal sequencing10aPenicillin V acylase10aPurification10aRhodotorula aurantiaca10aSubstrate specificity1 aKumar, Atul1 aPrabhune, Asmita1 aSuresh, C., G.1 aPundle, Archana  uhttps://library.ncl.res.in/content/characterization-smallest-active-monomeric-penicillin-v-acylase-new-source-yeast-001955nas a2200217   4500008004100000022001400041245019100055210006900246260007100315300001400386490000700400520106100407100001701468700001901485700002001504700002201524700002101546700002001567700001901587856013101606       2008                        eng d  a0897-475600aExtracellular bacterial synthesis of protein-functionalized ferromagnetic Co3O4 nanocrystals and imaging of self-organization of bacterial cells under stress after exposure to metal ions0 aExtracellular bacterial synthesis of proteinfunctionalized ferro  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcFEB  a1484-14910 v203 a<p>Co3O4, which crystallizes in the spinet phase at temperatures much higher than ambient temperatures, orders antiferromagnetically below its Neel temperature (similar to 40 K). However, in nanosize, it shows ferromagnetic ordering due to surface canting, disorder, imperfect oxygen atom coordination, etc. Here, for the first time, we report the synthesis of single-crystalline, ferromagnetic Co3O4 nanoparticles functionalized with proteins (size 5-7 nm) using cobalt acetate as precursor at room temperature in aqueous medium by a metal-tolerant marine bacterium isolated from the coast of the Arabian Sea. Energetically unfavorable change in the oxidation state of Co atoms from (+2 to +3) during synthesis by the bacterial strain was evidenced by X-ray photoelectron spectroscopy. The effect on the morphology of bacterial cells after exposure to the cobalt acetate was imaged by scanning electron microscopy showing cooperative, self-organized. structured colony formation, possibly due to the interbacterial communication under external stress.</p>1 aKumar, Umesh1 aShete, Ashvini1 aHarle, Arti, S.1 aKasyutich, Oksana1 aSchwarzacher, W.1 aPundle, Archana1 aPoddar, Pankaj  uhttps://library.ncl.res.in/content/extracellular-bacterial-synthesis-protein-functionalized-ferromagnetic-co3o4-nanocrystals-000652nas a2200145   4500008004100000022001400041245012500055210006900180260007300249300000900322490000800331100001600339700002000355856013100375       2008                        eng d  a0168-165600aPermeabilization effect of organic solvents on cell bound penicillin v acylase activity of Erwinia aroideae (DSMZ 30186)0 aPermeabilization effect of organic solvents on cell bound penici  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcOCT  aS3210 v1361 aKumar, Atul1 aPundle, Archana  uhttps://library.ncl.res.in/content/permeabilization-effect-organic-solvents-cell-bound-penicillin-v-acylase-activity-erwinia-002078nas a2200253   4500008004100000022001400041245019000055210006900245260007900314300001200393490000800405520106000413653002801473653002501501653002401526653002101550653002701571100001601598700001801614700001901632700002101651700002001672856013201692       2009                        eng d  a0273-228900aEffect of cultural conditions and media constituents on production of penicillin V acylase and CTAB treatment to enhance whole-cell enzyme activity of rhodotorula aurantiaca (NCIM 3425)0 aEffect of cultural conditions and media constituents on producti  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJUN  a463-4720 v1573 a<p>Penicillin V acylase (PVA) is a pharmaceutically important enzyme as it plays a vital role in the manufacture of semi-synthetic beta-lactam antibiotics. Rhodotorula aurantiaca (NCIM 3425) produced high levels of intracellular penicillin V acylase after 18 h at pH 8.0 and temperature 27 degrees C. Fructose was the best carbon source for PVA production, whereas tryptone was the best nitrogen source to produce the enzyme up to 170 and 1,088 IU/l of culture, respectively. Additionally, the cell-bound PVA activity was enhanced on treatment with cationic detergent. Whole-cell activity was found to be doubled (204%) on treatment of 0.01 g dry weight of cells with 50 mu g/ml solution of N-cetyl-N,N,N-trimethylammoniumbromide at pH 8.0 for 1 h at room temperature. Atomic force microscopy images of permeabilized cells show perturbation in the cell wall and offer first-ever visual illustration of surface structure modifications that occur during permeabilization of R. aurantiaca cells leading to enhancement in activity of intracellular enzyme.</p>10aAtomic force microscopy10aIntracellular enzyme10aPenicillin Vacylase10aPermeabilization10aRhodotorula aurantiaca1 aKumar, Atul1 aSingh, Sanjay1 aPoddar, Pankaj1 aPrabhune, Asmita1 aPundle, Archana  uhttps://library.ncl.res.in/content/effect-cultural-conditions-and-media-constituents-production-penicillin-v-acylase-and-ctab-001925nas a2200229   4500008004100000022001400041245013500055210006900190260007300259300001000332490000700342520105100349653002401400653002101424653001901445653002101464653002501485653002101510100001601531700002001547856012801567       2009                        eng d  a1381-117700aEffect of organic solvents on cell-bound penicillin V acylase activity of erwinia aroideae (DSMZ 30186): a permeabilization effect0 aEffect of organic solvents on cellbound penicillin V acylase act  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAY  a67-710 v573 a<p>Erwinia aroideae (DSMZ 30186) is a potential microbial culture to produce intracellular penicillin V acylase (PVA). The whole cell PVA activity was improved by permeabilization with various organic solvents. The cell-bound PVA activity showed an eightfold increase upon treatment with chloroform (5 mu L/mg(dry) (biomass)) for 10 min and diethyl ether (10 mu L/mg(dry) (biomass)) for 45 min. Hexane, toluene, ethyl acetate and dichloromethane enhanced the enzyme activity up to two-, six-, four- and two-fold, respectively; whereas, PVA activity declined drastically on permeabilization with acetone, pyridine and alcohols. The physicochemical properties of the organic solvents used for permeabilization were correlated with the change in activity. It was found that solvents with high hydrophobicity (log P &gt; 0.68) and lower dielectric constant (&lt; 9) were relatively effective in increasing PVA activity. These results allow systematic selection of suitable solvent for best performance. (c) 2008 Elsevier B.V. All rights reserved.</p>10adielectric constant10aErwinia aroideae10aHydrophobicity10aOrganic solvents10aPenicillin V acylase10aPermeabilization1 aKumar, Atul1 aPundle, Archana  uhttps://library.ncl.res.in/content/effect-organic-solvents-cell-bound-penicillin-v-acylase-activity-erwinia-aroideae-dsmz-002493nas a2200229   4500008004100000022001400041245010300055210006900158260006900227300001200296490000700308520163100315653002501946653002501971653002501996653002702021100001602048700002302064700002502087700002002112856013102132       2009                        eng d  a1011-134400aRhodotorula aurantiaca penicillin V acylase: active site characterization and fluorometric studies0 aRhodotorula aurantiaca penicillin V acylase active site characte  aPO BOX 564, 1001 LAUSANNE, SWITZERLANDbELSEVIER SCIENCE SAcNOV  a109-1160 v973 a<p>Penicillin V acylase (PVA), a member of newly evolved Ntn-hydrolase superfamily, is a pharmaceutically important enzyme to produce 6-aminopenicillanic acid. Active site characterization of recently purified monomeric PVA from Rhodotorula aurantiaca (Ra-PVA), the yeast source, showed the involvement of serine and tryptophan in the enzyme activity. Modification of the protein with serine and tryptophan specific reagents such as PMSF and NBS showed partial loss of PVA activity and substrate protection. Ra-PVA was found to be a multi-tryptophan protein exhibiting one tryptophan, in native and, four in its denatured condition. Various solute quenchers and substrate were used to probe the microenvironment of the putative reactive tryptophan through fluorescence quenching. The results obtained indicate that the tryptophan residues of Ra-PVA were largely buried in hydrophobic core of the protein matrix. Quenching of the fluorescence by acrylamide was collisional. Acrylamide was the most effective quencher amongst all the used quenchers, which quenched 71.6% of the total intrinsic fluorescence of the protein, at a very less final concentration of 0.1 M. Surface tryptophan residues were found to have predominantly more electropositively charged amino acids around them, however differentially accessible for ionic quenchers. Denaturation led to shift lambda(max) from 336, in native state, to 357 nm and more exposed to the solvent, consequently increase in fluorescence quenching with all quenchers. This is an attempt towards the conformational studies of Ra-PVA. (C) 2009 Elsevier B.V. All rights reserved.</p>10aactive site residues10aFluorometric studies10aPenicillin V acylase10aRhodotorula aurantiaca1 aKumar, Atul1 aGowda, Nagaraj, M.1 aGaikwad, Sushama, M.1 aPundle, Archana  uhttps://library.ncl.res.in/content/rhodotorula-aurantiaca-penicillin-v-acylase-active-site-characterization-and-fluorometric-001476nas a2200289   4500008004100000022001400041245011400055210006900169260007600238300001200314490000700326520044800333653002000781653002200801653001900823653002200842653002000864653002000884100002900904700001800933700001900951700002100970700002000991700002401011700001901035856013201054       2012                        eng d  a1744-309100aCrystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis0 aCrystallization and Xray structure analysis of a thermostable pe  aCOMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USAbWILEY-BLACKWELLcMAR  a273-2770 v683 a<p>{The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C2221, with unit-cell parameters a = 72.9</p>10acalcium binding10adisulfide bridges10aNtn hydrolases10aorthorhombic form10atetragonal form10aThermostability1 aVarshney, Nishant, Kumar1 aKumar, Suresh1 aIgnatova, Zoya1 aPrabhune, Asmita1 aPundle, Archana1 aDodson, Eleanor, J.1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/crystallization-and-x-ray-structure-analysis-thermostable-penicillin-g-acylase-alcaligenes-002188nas a2200277   4500008004100000022001400041245013600055210006900191260011100260300001200371490000600383520117200389653001801561653001801579653000901597653001301606653001801619653001101637100001701648700002401665700002701689700003101716700002001747700001901767856012401786       2012                        eng d  a1573-413700aGreen approach towards size controlled synthesis of biocompatible antibacterial metal nanoparticles in aqueous phase using lysozyme0 aGreen approach towards size controlled synthesis of biocompatibl  aEXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATESbBENTHAM SCIENCE PUBL LTDcFEB  a130-1400 v83 a<p>Inspired by array of proteins present in nature, we choose lysozyme (hen egg protein) as a model system to synthesize nanoparticles of noble metals to understand the mechanism of interaction as well as to use them for potential applications such as potent antibacterial agents. Lysozyme is a very well studied biomolecule containing aromatic amino acids like tryptophan and tyrosine. Tyrosine has phenoxy group which is considered to be responsible for interacting with the metal ions. Lysozyme can be suitably modified by treatment with N-bromosuccinimide/N-acetylimidazole to obtain tight control over size distribution of nanoparticles. Here we report the direct synthesis of nanocrystals of gold and silver at controlled pH and light conditions without using any known reducing agents. Out of these, synthesis of gold nanoparticles is assisted by the presence of low concentration of Ag+ ions through the galvanic exchange. It is remarkable to note that the structure of protein is not changed drastically as seen by the FTIR studies. As-synthesized lysozyme capped nanoparticles prepared by this method are biocompatible and retain antibacterial property.</p>10aAntibacterial10aBiocompatible10aGold10alysozyme10aNanoparticles10aSilver1 aKumar, Umesh1 aRanjan, Amaresh, K.1 aSharan, Chandrashekhar1 aHardikar, Anandwardhan, A.1 aPundle, Archana1 aPoddar, Pankaj  uhttps://library.ncl.res.in/content/green-approach-towards-size-controlled-synthesis-biocompatible-antibacterial-metal-002266nas a2200241   4500008004100000022001400041245011000055210006900165260007300234300000800307490000700315520137800322653001601700653002001716653001801736653002501754653002501779100002901804700002601833700001901859700002001878856012601898       2015                        eng d  a0141-813000aPenicillin V acylase from pectobacterium atrosepticum exhibits high specific activity and unique kinetics0 aPenicillin V acylase from pectobacterium atrosepticum exhibits h  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcAUG  a1-70 v793 a<p>Penicillin V acylases (PVAs, E.C.3.5.11) belong to the Ntn hydrolase super family of enzymes that catalyze the deacylation of the side chain from phenoxymethyl penicillin (penicillin V). Penicillin acylases find use in the pharmaceutical industry for the production of semi-synthetic antibiotics. PVAs employ the N-terminal cysteine residue as catalytic nucleophile and are structurally and evolutionarily related to bile salt hydrolases (BSHs). Here, we report the cloning and characterization of a PVA enzyme from the Gram-negative plant pathogen, Pectobacterium atrosepticum (PaPVA). The enzyme was cloned and expressed in Escherichia coli attaining a very high yield (250 mg/l) and a comparatively high specific activity (430 IU/mg). The enzyme showed marginally better pH and thermo-stability over PVAs characterized from Gram-positive bacteria. The enzyme also showed enhanced activity in presence of organic solvents and detergents. The enzyme kinetics turned out to be significantly different from that of previously reported PVAs, displaying positive cooperativity and substrate inhibition. The presence of bile salts had a modulating effect on PaPVA activity. Sequence analysis and characterization reveal the distinctive nature of these enzymes and underscore the need to study PVAs from Gram-negative bacteria. (C) 2015 Elsevier B.V. All rights reserved.</p>10aCooperative10aEnzyme kinetics10aGram-negative10aPenicillin V acylase10aSubstrate inhibition1 aAvinash, Vellore, Sunder1 aRamasamy, Sureshkumar1 aSuresh, C., G.1 aPundle, Archana  uhttps://library.ncl.res.in/content/penicillin-v-acylase-pectobacterium-atrosepticum-exhibits-high-specific-activity-and-002452nas a2200265   4500008004100000022001400041245015600055210006900211260009500280300001000375490000800385520139300393653002201786653002801808653002301836653001601859653002801875100002901903700002601932700001801958700002001976700003401996700002602030856013002056       2016                        eng d  a1047-847700aStructural analysis of a penicillin V acylase from pectobacterium atrosepticum confirms the importance of two Trp residues for activity and specificity0 aStructural analysis of a penicillin V acylase from pectobacteriu  a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcFEB  a85-940 v1933 a<p>Penicillin V acylases (PVA) catalyze the deacylation of the beta-lactam antibiotic phenoxymethylpenicillin (Pen V). They are members of the Ntn hydrolase family and possess an N-terminal cysteine as the main catalytic nucleophile residue. They form the evolutionarily related cholylglycine hydrolase (CGH) group which includes bile salt hydrolases (BSH) responsible for bile deconjugation. Even though a few PVA and BSH structures have been reported, no structure of a functional PVA from Gram-negative bacteria is available. Here, we report the crystal structure of a highly active PVA from Gram-negative Pectobacterium atrosepticum (PaPVA) at 2.5 angstrom resolution. Structural comparison with PVAs from Gram-positive bacteria revealed that PaPVA had a distinctive tetrameric structure and active site organization. In addition, mutagenesis of key active site residues and biochemical characterization of the resultant variants elucidated the role of these residues in substrate binding and catalysis. The importance of residue Trp23 and Trp87 side chains in binding and correct positioning of Pen V by PVAs was confirmed using mutagenesis and substrate docking with a 15 ns molecular dynamics simulation. These results establish the unique nature of Gram-negative CGHs and necessitate further research about their substrate spectrum. (C) 2015 Elsevier Inc. All rights reserved.</p>10aAromatic stacking10aCholylglycine hydrolase10amolecular dynamics10aMutagenesis10aOligomeric interactions1 aAvinash, Vellore, Sunder1 aPanigrahi, Priyabrata1 aChand, Deepak1 aPundle, Archana1 aSuresh, Cheravakattu, Gopalan1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/structural-analysis-penicillin-v-acylase-pectobacterium-atrosepticum-confirms-importance-002038nas a2200169   4500008004100000245015500041210006900196260000800265300001000273490000700283520134800290100002901638700002701667700002201694700002001716856013201736       2017                        eng d00aBiotransformation of penicillin V to 6-aminopenicillanic acid using immobilized whole cells of E. coli expressing a highly active penicillin V acylase0 aBiotransformation of penicillin V to 6aminopenicillanic acid usi  cJAN  a52-570 v473 aThe production of 6-aminopenicillanic acid (6-APA) is a key step in the manufacture of semisynthetic antibiotics in the pharmaceutical industry. The penicillin G acylase from Escherichia coli has long been utilized for this purpose. However, the use of penicillin V acylases (PVA) presents some advantages including better stability and higher conversion rates. The industrial application of PVAs has so far been limited due to the nonavailability of suitable bacterial strains and cost issues. In this study, whole-cell immobilization of a recombinant PVA enzyme from Pectobacterium atrosepticum expressed in E. coli was performed. Membrane permeabilization with detergent was used to enhance the cell-bound PVA activity, and the cells were encapsulated in calcium alginate beads and cross-linked with glutaraldehyde. Optimization of parameters for the biotransformation by immobilized cells showed that full conversion of pen V to 6-APA could be achieved within 1 hr at pH 5.0 and 35 degrees C, till 4% (w/v) concentration of the substrate. The beads could be stored for 28 days at 4 degrees C with minimal loss in activity and were reusable up to 10 cycles with 1-hr hardening in CaCl2 between each cycle. The high enzyme productivity of the PVA enzyme system makes a promising case for its application for 6-APA production in the industry.1 aAvinash, Vellore, Sunder1 aChauhan, Palna, Dinesh1 aGaikwad, Shraddha1 aPundle, Archana  uhttps://library.ncl.res.in/content/biotransformation-penicillin-v-6-aminopenicillanic-acid-using-immobilized-whole-cells-e-coli02535nas a2200265   4500008004100000022001400041245013800055210006900193260000800262300001400270490000800284520159300292653003701885653001801922653001701940653002401957653002101981100002902002700002202031700002602053700002402079700001402103700002002117856013202137       2017                        eng d  a0175-759800aPenicillin V acylases from gram-negative bacteria degrade N-acylhomoserine lactones and attenuate virulence in Pseudomonas aeruginosa0 aPenicillin V acylases from gramnegative bacteria degrade Nacylho  cMAR  a2383-23950 v1013 a<p>Virulence pathways in gram-negative pathogenic bacteria are regulated by quorum sensing mechanisms, through the production and sensing of N-acylhomoserine lactone (AHL) signal molecules. Enzymatic degradation of AHLs leading to attenuation of virulence (quorum quenching) could pave the way for the development of new antibacterials. Penicillin V acylases (PVAs) belong to the Ntn hydrolase superfamily, together with AHL acylases. PVAs are exploited widely in the pharmaceutical industry, but their role in the natural physiology of their native microbes is not clearly understood. This report details the characterization of AHL degradation activity by homotetrameric PVAs from two gram-negative plant pathogenic bacteria, Pectobacterium atrosepticum (PaPVA) and Agrobacterium tumefaciens (AtPVA). Both the PVAs exhibited substrate specificity for degrading long-chain AHLs. Exogenous addition of these enzymes into Pseudomonas aeruginosa greatly diminished the production of elastase and pyocyanin and biofilm formation and increased the survival rate in an insect model of acute infection. Subtle structural differences in the PVA active site that regulate specificity for acyl chain length have been characterized, which could reflect the evolution of AHL-degrading acylases in relation to the environment of the bacteria that produce them and also provide strategies for enzyme engineering. The potential for using these enzymes as therapeutic agents in clinical applications and a few ideas about their possible significance in microbial physiology have also been discussed.</p>10aN-acylhomoserine lactone acylase10aNtn hydrolase10apathogenesis10aPenicillin Vacylase10aQuorum quenching1 aSunder, Avinash, Vellore1 aUtari, Putri, Dwi1 aRamasamy, Sureshkumar1 avan Merkerk, Ronald1 aQuax, Wim1 aPundle, Archana  uhttps://library.ncl.res.in/content/penicillin-v-acylases-gram-negative-bacteria-degrade-n-acylhomoserine-lactones-and-attenuate02147nas a2200193   4500008004100000022001400041245014800055210006900203260000900272300001600281490000600297520140000303100002101703700002901724700003001753700002601783700002001809856012401829       2020                        eng d  a2470-134300aProcess development for 6-aminopenicillanic acid production using lentikats-encapsulated escherichia coli cells expressing penicillin V acylase0 aProcess development for 6aminopenicillanic acid production using  cNOV   a28972-289760 v53 a<p>Penicillin V acylase (PVA, EC 3.5.1.11) hydrolyzes the side chain of phenoxymethylpenicillin (Pen V) and finds application in the manufacture of the pharmaceutical intermediate 6-aminopenicillanic acid (6-APA). Here, we report the scale-up of cultivation of Escherichia coli whole cells expressing a highly active PVA from Pectobacterium atrosepticum and their encapsulation in polyvinyl alcohol-poly(ethylene glycol) Lentikats hydrogels. A biocatalytic process for the hydrolysis of 2% (w/v) Pen V was set up in a 2 L reactor using the Lentikats-immobilized whole cells, with a customized setup to enable continuous downstream processing of the reaction products. The biocatalytic reaction afforded complete conversion of Pen V for 10 reaction cycles, with an overall 90% conversion up to 50 cycles. The bioprocess was further scaled up to the pilot-scale at 10 L, enabling complete conversion of Pen V to 6-APA for 10 cycles. The 6-APA and phenoxy acetic acid products were recovered from downstream processing with isolated yields of 85-90 and 87-92%, respectively. Immobilization in Lentikats beads improved the stability of the whole cells on storage, maintaining 90-100% activity and similar conversion efficiency after 3 months at 4 degrees C. The robust PVA biocatalyst can be employed in a continuous process to provide a sustainable route for bulk 6-APA production from Pen V.</p>
1 aSawant, Amol, M.1 aSunder, Avinash, Vellore1 aVamkudoth, Koteswara, Rao1 aRamasamy, Sureshkumar1 aPundle, Archana  uhttps://library.ncl.res.in/content/process-development-6-aminopenicillanic-acid-production-using-lentikats-encapsulated