01941nas a2200241   4500008004100000022001400041245015600055210006900211260007300280300001200353490000700365520100800372653002601380653003301406653002201439653001801461653001701479653001001496100002401506700002901530700001701559856012301576       2008                        eng d  a1369-703X00aIntegrated process for extraction and purification of alcohol dehydrogenase from Baker's yeast involving precipitation and aqueous two phase extraction0 aIntegrated process for extraction and purification of alcohol de  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAR  a414-4200 v383 a<p>The potential of aqueous two phase extraction for the purification of alcohol dehydrogenase (ADH) from Baker's yeast (Saccharomyces cerevisiae) is demonstrated. An integrated process involving precipitation followed by aqueous two phase extraction (ATPE) is used for effective recovery of the enzyme. This is carried out in two schemes. In the first scheme, ammonium sulphate precipitation is carried out followed by ATPE of the precipitate after suspending it in buffer. While the second scheme involves polyethylene glycol precipitation followed by ATPE of the supernatant. The effect of various process parameters such as molecular weight of polymer, tie line length, phase volume ratio and neutral salt is investigated for enhancing the activity recovery of ADH. First scheme resulted in about 85% enzyme activity recovery of ADH with purification factor of 4.2 while the second scheme about 90% enzyme activity recovery with 6.6-fold purification. (C) 2007 Elsevier B.V. All rights reserved.</p>10aAlcohol dehydrogenase10aaqueous two phase extraction10aenzyme extraction10aPrecipitation10aPurification10aYeast1 aMadhusudhan, M., C.1 aRaghavarao, K., S. M. S.1 aNene, Sanjay  uhttps://library.ncl.res.in/content/integrated-process-extraction-and-purification-alcohol-dehydrogenase-bakers-yeast-002723nas a2200325   4500008004100000022001400041245019400055210006900249260007300318300001200391490000700403520146800410653003301878653001501911653002601926653002501952653002501977653001702002653003502019653002602054653001202080100001802092700003102110700002002141700002402161700002902185700003002214700002502244856012802269       2012                        eng d  a0927-776500aAdsorption induced enzyme denaturation: the role of protein surface in adsorption induced protein denaturation on allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymers0 aAdsorption induced enzyme denaturation the role of protein surfa  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a184-1900 v903 a<p>The effects of protein size on adsorption and adsorption-induced denaturation of proteins on copolymers of allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) have been studied. Different responses were observed for the amount of protein adsorbed and denatured on the polymer surface for different proteins (trypsin, alchol dehydrogenase from baker's yeast (YADH), glucose dehydrogenase (GDH) from Gluconobacter cerinus, and alkaline phosphates from calf intestinal mucosa (CIAP). Protein adsorption on the copolymer with 25% crosslink density (AGE-25) was dependent not only on the size of the protein but also on the presence of glycoside residues on the protein surface. Adsorption and denaturation of proteins follows the order YADH &gt; trypsin &gt; GDH &gt;&gt; CIAP although the molecular weights of the proteins follow the order YADH &gt; CIAP &gt; GDH &gt; trypsin. The lack of correlation between amount of adsorbed protein and its molecular weight was due to the presence of glycoside residues on CIAP and GDH which protect the enzyme surface from denaturation. Enzyme stabilities in aqueous solutions of 1-cyclohexyl-2-pyrrolidinone (CHP) correlate well with the trend in denaturation by the copolymer, strongly suggesting that hydrophobic interactions play a major role in protein binding and the mechanism of protein denaturation is similar to that for water-miscible organic solvents. (C) 2011 Elsevier B.V. All rights reserved.</p>10a1-Cyclohexyl-2-pyrrolidinone10aAdsorption10aAlcohol dehydrogenase10aAlkaline phosphatase10aallyl glycidyl ether10aDenaturation10aethylene glycol dimethacrylate10aGlucose dehydrogenase10aTrypsin1 aThudi, Lahari1 aJasti, Lakshmi, Swarnalath1 aSwarnalatha, Y.1 aFadnavis, Nitin, W.1 aMulani, Khudbudin, Baban1 aDeokar, Sarika, Babasaheb1 aPonrathnam, Surendra  uhttps://library.ncl.res.in/content/adsorption-induced-enzyme-denaturation-role-protein-surface-adsorption-induced-protein-0