Gly or Ala substitutions for Pro210Thr211Asn212 at the β8-β9 turn of subtilisin Carlsberg increase the catalytic rate and decrease thermostability

► We substituted Gly or Ala for Pro-Thr-Asn at β8-β9 turn of subtilisin Carlsberg (sC). ► This turn is located apart from the active site. ► These mutations increased kcat for peptide hydrolysis and decreased thermostability. ► P210G mutation had the largest effects among single Gly substitutions for PTN residues. ► Positive correlations were found between kcat and thermal inactivation rates.