Effect of protease digestion on the activity of sugardepleted enzymes prepared with endo-β-N-acetylglucosaminidase from Flavobacterium sp

Kenji Yamamoto, Kaoru Takegawa, Hidehiko Kumagai, Tatsurokuro Tochikura

研究成果: Contribution to journalArticle査読

18 被引用数 (Scopus)

抄録

Endo-β-N-acetylglucosaminidase, purified to homogeneity from the culture filtrate of a Flavobacterium sp., liberated the carbohydrate chains from yeast invertase. About 90% of the carbohydrate associated with this glycoprotein was removed by the endo-β-N-acetylglucosaminidase. The native and carbohydrate-depleted enzymes were compared and found to exhibit similar catalytic activities, thermal stabilities and pH-activity profiles. However, the carbohydrate-depleted invertase was more susceptible to proteases with relatively broad specificities such as subtilisin and pronase, as found on examination of the enzyme activity and electrophoresis. On the other hand, trypsin did not have such an effect on the enzyme activities of the native and carbohydrate-depleted enzymes. The endo-β-N-acetylglucosaminidase also released carbohydrate chains from the purified β-N-acetylhexosaminidase of Penicillium oxalicum. Although the native and carbohydrate-depleted β-N-acetylhexosaminidases did not differ significantly in their stabilities or pH-activity profiles, the carbohydrate-depleted form was more susceptible to proteolysis by subtilisin, pronase and trypsin. From these results, it would appear that the carbohydrate of a glycosylated enzyme plays a role in protecting the enzyme from proteolysis.

本文言語英語
ページ(範囲)1481-1487
ページ数7
ジャーナルAgricultural and Biological Chemistry
51
6
DOI
出版ステータス出版済み - 6 1987
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学、遺伝学、分子生物学(全般)
  • 農業および生物科学(全般)

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