Effect of deglycosylation of polymannose chains on the properties of yeast external invertase

Kaoru Takegawa, Satoshi Miki, Shojiro Iwahara

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

α-Mannosidase from Cellulomonas sp. released about 70% of the polymannose chains from yeast external invertase. Native and mannose-depleted yeast invertases were compared with regard to various enzymatic properties. It was found that their catalytic activity and thermal and pH stability were identical. However, the mannose-depleted invertase was more sensitive to proteinases such as pronase and subtilisin. The mannose-depleted invertase was less stable than the native enzyme when incubated with sodium dodecyl sulfate. These results show that the polymannose chains of yeast invertase contribute to the high stability of the enzyme.

Original languageEnglish
Pages (from-to)131-133
Number of pages3
JournalJournal of Fermentation and Bioengineering
Volume70
Issue number2
DOIs
Publication statusPublished - Jan 1 1990
Externally publishedYes

Fingerprint

beta-Fructofuranosidase
Yeast
Yeasts
Mannose
Enzymes
Sodium dodecyl sulfate
Cellulomonas
Mannosidases
Catalyst activity
Subtilisin
Enzyme Stability
Pronase
Sodium Dodecyl Sulfate
Peptide Hydrolases
Hot Temperature
polymannose

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Effect of deglycosylation of polymannose chains on the properties of yeast external invertase. / Takegawa, Kaoru; Miki, Satoshi; Iwahara, Shojiro.

In: Journal of Fermentation and Bioengineering, Vol. 70, No. 2, 01.01.1990, p. 131-133.

Research output: Contribution to journalArticle

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