{"refrec":{"BRefID":280847,"RR":"Srimathi, S.; Jayaraman, G.; Feller, G.; Danielsson, B.; Narayanan, P.R. (2007). Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis. Extremophiles 11(3): 505-515. https://dx.doi.org/10.1007/s00792-007-0062-5","BEntID":272866,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". Extremophiles 11(3): 505-515. https://dx.doi.org/10.1007/s00792-007-0062-5","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Srimathi, S.; Jayaraman, G.; Feller, G.; Danielsson, B.; Narayanan, P.R.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Srimathi, S. et al.","Englishabstract":"The halotolerance of a cold adapted α-amylase from the psychrophilic bacterium Pseudoalteromonas haloplanktis (AHA) was investigated. AHA exhibited hydrolytic activity over a broad range of NaCl concentrations (0.01–4.5 M). AHA showed 28% increased activity in 0.5–2.0 M NaCl compared to that in 0.01 M NaCl. In contrast, the corresponding mesophilic (Bacillus amyloliquefaciens) and thermostable (B. licheniformis) α-amylases showed a 39 and 46% decrease in activity respectively. Even at 4.5 M NaCl, 80% of the initial activity was detected for AHA, whereas the mesophilic and thermostable enzymes were inactive. Besides an unaltered fluorescence emission and secondary structure, a 10°C positive shift in the temperature optimum, a stabilization factor of >5 for thermal inactivation and a ΔTm of 8.3°C for the secondary structure melting were estimated in 2.7 M NaCl. The higher activation energy, half-life time and Tm indicated reduced conformational dynamics and increased rigidity in the presence of higher NaCl concentrations. A comparison with the sequences of other halophilic α-amylases revealed that AHA also contains higher proportion of small hydrophobic residues and acidic residues resulting in a higher negative surface potential. Thus, with some compromise in cold activity, psychrophilic adaptation has also manifested halotolerance to AHA that is comparable to the halophilic enzymes.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis","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":"acidic protein; Pseudoalteromonas haloplanktis alpha-amylase;halophilic; halotolerance; psychrophilic; stability","OtherDescriptors":null,"Notes":null,"AnaPub":2007,"MonPub":null,"DateUpdate":"2022-05-02","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000246353300010","VABBcode":null,"OpenAcc":0,"DOI":"10.1007/s00792-007-0062-5"},"refs":null,"anarec":{"AnaID":280847,"PubliDate":2007,"Pagination":"505-515","XtraPublOfAnaID":null,"ISBN":null,"Volume":"11","Issue":"3","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":218588,"SerRR":"Extremophiles. Springer: Tokyo. 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