and gradually recovering its enzymatic activity at room temperature may therefore be desirable from an industrial point of view by modeling u03b2 1 3 1 4 celloheptaose representing the original substrate lichenan fitted neatly into the catalytic cleft of tfs w203f but laminarihexose representative of laminarin did not fit well and indeed collided with the residues at the active site the three sequential u03b2 1 3 glucose moieties in the modeled laminarihexose did however fit neatly into the active site of tfs w203f because the tfs w203f tmlam cd showed an improvement a 3 6 fold increase in specific activity against laminarin as compared to tmlam cd alone and because we have recently demonstrated that laminaritriose is the major product of tmlam cd toward the substrate laminarin jeng et al 2011 j biol chem 286 45030 45040 the tfs w203f domain in tfs w203f tmlam cd may play a role in capturing the product laminaritriose which results in the facilitation and enhancement of the catalytic activity of tfs w203f tmlam cd toward laminarin however a slight decrease 2 6 u02dc 3 7 fold in binding affinity with lichenan and laminarin was also observed in the hybrid enzyme as compared with.