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(Tokyo)"},{"key":"10.1016\/S1389-1723(04)00290-7_BIB85","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1046\/j.0014-2956.2002.02631.x","article-title":"Cold adaptation of xylose isomerase from Thermus thermophilus through random PCR mutagenesis. Gene cloning and protein characterization","volume":"269","author":"Lonn","year":"2002","journal-title":"Eur. J. 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Chem"},{"key":"10.1016\/S1389-1723(04)00290-7_BIB95","doi-asserted-by":"crossref","first-page":"10723","DOI":"10.1021\/bi010808b","article-title":"Activity and stability of a thermostable \u03b1-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation","volume":"40","author":"Fitter","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/S1389-1723(04)00290-7_BIB96","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/abbi.1998.0830","article-title":"A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima","volume":"358","author":"Ichikawa","year":"1998","journal-title":"Arch. Biochem. 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