Characterization of Bacillus sp. endo-beta-N-acetylglucosaminidase and its application to deglycosylation of hen ovomucoid. 1998

K Yamamoto, and T Tanaka, and K Fujimori, and C S Kang, and H Ebihara, and J Kanamori, and S Kadowaki, and T Tochikura, and H Kumagai
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-01, Japan.

A bacterial strain isolated from soil and identified as a Bacillus species produced two endo-beta-N-acetylglucosaminidases in the culture broth when it was cultivated on medium containing only hen ovomucoid. Almost no production of the enzymes occurred when the bacterium was grown on glucose medium. The two endo-beta-N-acetylglucosaminidases, named Endo-BI and Endo-BII, were separated and purified to homogeneity by preparative gel electrophoresis after partial purification by column chromatography on DEAE-resins. Endo-BI hydrolysed oligosaccharides of both hen ovalbumin and ovomucoid. In contrast, Endo-BII could act only on oligosaccharides of hen ovalbumin and showed almost no activity towards those of hen ovomucoid. Deglycosylation of hen ovomucoid was performed with the partly purified endo-beta-N-acetylglucosaminidase preparation, with the aid of contaminating beta-N-acetylhexosaminidase. The deglycosylated ovomucoid exhibited no changes in trypsin inhibitory activity but was very unstable to heat treatment in comparison with native ovomucoid. These results suggest that oligosaccharides of ovomucoid have an important role in the stabilization of the protein against heat.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009844 Oligosaccharides Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form. Oligosaccharide
D010059 Ovomucin A heterogeneous mixture of glycoproteins responsible for the gel structure of egg white. It has trypsin-inhibiting activity. Ovomucoid
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D003470 Culture Media Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN. Media, Culture
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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