02033nas a2200253   4500008004100000022001400041245014000055210006900195260005700264300001400321490000700335520111700342653001301459653002001472653001401492653001801506653001701524653002301541100002901564700001601593700001501609700002401624856013101648       2012                        eng d  a1590-426100aCharacterization of a new bacillus cereus ATUAVP1846 strain producing penicillin V acylase, and optimization of fermentation parameters0 aCharacterization of a new bacillus cereus ATUAVP1846 strain prod  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcSEP  a1287-12930 v623 a<p>Penicillin acylases are involved chiefly in the industrial production of semisynthetic penicillins, which remain the most widely used group of antibiotics. We have isolated a new bacterial strain ATUAVP1846 that produces penicillin V acylase (PVA). Phylogenetic analysis using 16S rRNA sequencing showed 99.37% homology with Bacillus cereus. Maximum PVA production was observed with B. cereus ATUAVP1846 at 30A degrees C, pH 7 after 24 h fermentation time under submerged conditions. Highest enzyme productivity was achieved using sucrose as carbon source, and tryptone and ammonium hydrogen phosphate as nitrogen sources. Minimal medium containing 0.4% glucose and 0.3% ammonium hydrogen phosphate was found to be optimal for maximum PVA production from B. cereus ATUAVP1846. The crude enzyme from B. cereus ATUAVP1846 was partially purified using ammonium sulfate fractionation and showed highest enzymatic activity in the hydrolysis of penicillin V at 40A degrees C and pH 6. The crude enzyme preparation also showed unique substrate specificity, preferring ampicillin and cephalexin over penicillin V.</p>10a16S rRNA10aBacillus cereus10aisolation10aNtn hydrolase10aOptimization10aPenicillin acylase1 aSunder, Avinash, Vellore1 aKumar, Atul1 aNaik, Neha1 aPundle, Archana, V.  uhttps://library.ncl.res.in/content/characterization-new-bacillus-cereus-atuavp1846-strain-producing-penicillin-v-acylase-and-002185nas a2200265   4500008004100000022001400041245009100055210006900146260007300215300001000288490000700298520124000305653002201545653003601567653001801603653002301621100002401644700002501668700001901693700002101712700002501733700002001758700002401778856011701802       2012                        eng d  a0141-813000aPurification and characterization of YxeI, a penicillin acylase from Bacillus subtilis0 aPurification and characterization of YxeI a penicillin acylase f  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcJAN  a25-300 v503 a<p>The paper reports the purification and characterization of the first penicillin acylase from Bacillus subtilis. YxeI, the protein annotated as hypothetical, coded by the gene yxeI in the open reading frame between iol and hut operons in B. subtilis was cloned and expressed in Eshcherichia coli, purified and characterized. The purified protein showed measurable penicillin acylase activity with penicillin V. The enzyme was a homotetramer of 148 kDa. The apparent Km of the enzyme for penicillin V and the synthetic substrate 2-nitro-5-(phenoxyacetamido)-benzoic acid was 40 mM and 0.63 mM, respectively, and the association constants were 8.93 x 10(2) M-1 and 2.51 x 10(5) M-1, respectively. It was inhibited by cephalosporins and conjugated bile salts, substrates of the closely related bile acid hydrolases. It had good sequence homology with other penicillin V acylases and conjugated bile acid hydrolases, members of the Ntn hydrolase family. The N-terminal nucleophile was a cysteine which is revealed by a simple removal of N-formyl-methionine. The activity of the protein was affected by high temperature, acidic pH and the presence of the denaturant guanidine hydrochloride. (C) 2011 Elsevier B.V. All rights reserved.</p>10aBacillus subtilis10aConjugated bile acid hydrolases10aNtn hydrolase10aPenicillin acylase1 aRathinaswamy, Priya1 aGaikwad, Sushama, M.1 aSuresh, C., G.1 aPrabhune, Asmita1 aBrannigan, James, A.1 aDodson, Guy, G.1 aPundle, Archana, V.  uhttps://library.ncl.res.in/content/purification-and-characterization-yxei-penicillin-acylase-bacillus-subtilis-0