02072nas a2200265   4500008004100000022001400041245011400055210006900169260011700238300001000355490000600365520106900371653002801440653001501468653003701483653001701520653001401537653001101551100003101562700002401593700002001617700002201637700002301659856012401682       2007                        eng d  a0973-626300aImmobilization of invertase on functionalized mesoporous silica and properties of the immobilized biocatalyst0 aImmobilization of invertase on functionalized mesoporous silica   aSECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIAbRESEARCH JOURNAL BIOTECHNOLOGYcFEB  a12-170 v23 a<p>Invertase, which catalyses the hydrolysis of sucrose, is one of the simplest commercial carbohydrases and is used for the production of invert syrup (mixture of glucose and fructose). Fructose is the sweetest natural sugar having beneficial medicinal effects and is emerging as an alternative sweetener to sucrose in the pharmaceutical industry. beta fructofuranosidase (E C 3.2.1.26) purified from Kluyveromyces marxianus NCYC 2675, a thermotolerant yeast, was immobilized on functionalized mesoporous silica SBA- 15. Attempts were made to immobilize invertase on functionalized silicalite and cross linked with glutaraldehyde so as to obtain a highly active and stable immobilized enzyme preparation suitable for commercial exploitation. Cross linked enzyme silica complex as well as enzyme silica complex showed very good temperature and pH stability. Extrudates of the mesoporous silica also showed similar results. Bound enzyme showed excellent stability to repeated use and retained 90% of its initial activity after ten cycles of reuse in batch mode.</p>10abeta fructofuranosidase10aextrudates10afunctionalized mesoporous silica10aInvert syrup10ainvertase10aSBA-151 aPrabhune, Asmita, Ashutosh1 aSulabha, Karandikar1 aArchana, Pundle1 aShilpa, Deshpande1 aSanjeevani, Pardhy  uhttps://library.ncl.res.in/content/immobilization-invertase-functionalized-mesoporous-silica-and-properties-immobilized02055nas a2200229   4500008004100000022001400041245017100055210006900226260011700295300001000412490000600422520111600428653001901544653002101563653001801584653002101602653002501623100001601648700001801664700002001682856012301702       2008                        eng d  a0973-626300aStudies on optimization of cultural conditions and effect of media constituents on production of intracellular penicillin V acylase from Erwinia aroideae (DSMZ 30186)0 aStudies on optimization of cultural conditions and effect of med  aSECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIAbRESEARCH JOURNAL BIOTECHNOLOGYcMAY  a26-300 v33 a<p>Penicillin V acylase (PVA) is a pharmaceutically important enzyme. Erwinia aroideae (DSMZ 30186) produced high levels of intracellular penicillin V acylase. Amongst various carbon sources used (2.0 %); fructose, galactose, sucrose and mannitol increased enzyme production up to 579, 544, 534 and 504 IU/g dry weight (DW), respectively, compared to minimal media (263 IU/g DW); however maximum PVA productivity (2796 IU/ L) was achieved using fructose. Ammonium ions escalated the enzyme production to 1266.9 IU/g DW; however sodium glutamate was the best nitrogen source for overall productivity of enzyme (2045 IU/ L). Cornsteep liquor and skim milk were used as supplements; 1.0 % cornsteep liquor and 3.0 % skim milk were optimum for the production of PVA up to 823 and 93 IU/g DW, respectively. Optimum cultural conditions for the production of PVA from E. aroideae were standardized. Erwinia aroideae produced 1543 IU/g DW penicillin V acylase in Erlenmeyer flasks (250 ml) containing 50 ml of minimal medium with 0.3% ammonium sulphate, pH 7. 0 at 28 degrees C and 180 rpm when incubated for 56 hr.</p>10acarbon sources10aErwinia aroideae10aintracellular10anitrogen sources10aPenicillin V acylase1 aAtul, Kumar1 aVivek, Lonkar1 aArchana, Pundle  uhttps://library.ncl.res.in/content/studies-optimization-cultural-conditions-and-effect-media-constituents-production-0