{"refrec":{"BRefID":281104,"RR":"<b>Hoyoux, A.; Jennes, I.; Dubois, P.; Genicot, S.; Dubail, F.; François, J.-M.; Baise, E.; Feller, G.; Gerday, C.</b> (2001). Cold-adapted β-galactosidase from the Antarctic psychrophile <i>Pseudoalteromonas haloplanktis</i>. <i>Appl. Environ. Microbiol. 67(4)</i>: 1529-1535. <a href=\"http://dx.doi.org/10.1128/AEM.67.4.1529-1535.2001\" target=\"_blank\">dx.doi.org/10.1128/AEM.67.4.1529-1535.2001</a>","BEntID":273123,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Appl. Environ. Microbiol. 67(4)</i>: 1529-1535. <a href=\"https://dx.doi.org/10.1128/AEM.67.4.1529-1535.2001\" target=\"_blank\">https://dx.doi.org/10.1128/AEM.67.4.1529-1535.2001</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Hoyoux, A.; Jennes, I.; Dubois, P.; Genicot, S.; Dubail, F.; François, J.-M.; Baise, E.; Feller, G.; Gerday, C.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Hoyoux, A. <i>et al.</i>","Englishabstract":"The β-galactosidase from the Antarctic gram-negative bacterium <i>Pseudoalteromonas haloplanktis</i> TAE 79 was purified to homogeneity. The nucleotide sequence and the NH<sub>2</sub>-terminal amino acid sequence of the purified enzyme indicate that the β-galactosidase subunit is composed of 1,038 amino acids with a calculated <i>M</i> <sub>r</sub> of 118,068. This β-galactosidase shares structural properties with <i>Escherichia coli</i> β-galactosidase (comparable subunit mass, 51% amino sequence identity, conservation of amino acid residues involved in catalysis, similar optimal pH value, and requirement for divalent metal ions) but is characterized by a higher catalytic efficiency on synthetic and natural substrates and by a shift of apparent optimum activity toward low temperatures and lower thermal stability. The enzyme also differs by a higher pI (7.8) and by specific thermodynamic activation parameters. <i>P. haloplanktis</i> β-galactosidase was expressed in <i>E. coli</i>, and the recombinant enzyme displays properties identical to those of the wild-type enzyme. Heat-induced unfolding monitored by intrinsic fluorescence spectroscopy showed lower melting point values for both <i>P. haloplanktis</i>wild-type and recombinant β-galactosidase compared to the mesophilic enzyme. Assays of lactose hydrolysis in milk demonstrate that <i>P. haloplanktis</i> β-galactosidase can outperform the current commercial β-galactosidase from <i>Kluyveromyces marxianus</i>var. lactis, suggesting that the cold-adapted β-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Cold-adapted β-galactosidase from the Antarctic psychrophile <i>Pseudoalteromonas haloplanktis</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2001,"MonPub":null,"DateUpdate":"2016-10-26","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000167865500020","VABBcode":null,"OpenAcc":0,"DOI":"10.1128/AEM.67.4.1529-1535.2001"},"refs":null,"anarec":{"AnaID":281104,"PubliDate":2001,"Pagination":"1529-1535","XtraPublOfAnaID":null,"ISBN":null,"Volume":"67","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42360,"SerRR":"Applied and Environmental Microbiology. 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