Protein endoglycosidases are useful for biocatalytic alteration of glycans on protein surfaces, but the currently limited selectivity of endoglycosidases has prevented effective manipulation of certain N-linked glycans widely found in nature. Here we reveal that a bacterial endoglycosidase from Streptococcus pyogenes , EndoS, is complementary to other known endoglycosidases (EndoA, EndoH) used for current protein remodeling. It allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans. This biocatalytic activity now addresses previously refractory antibody glycoforms.

Soluble and ionically-bound peroxidases have been obtained from the pulp and peel of Conference pears. The peel soluble fraction contained the highest level of peroxidase activity. The peel peroxidases, both soluble and ionically bound, were particularly heat stable. Following heat inactivation, regeneration of enzymic activity was observed for the peel peroxidases and soluble pulp enzymes. Plots of the percentage of heat inactivation for the pear peroxidases against heating time were non-linear.