A novel ribonuclease from fruiting bodies of the common edible mushroom Pleurotus eryngii.

Pleurotus eryngii

Gut & microbiome

SpeciesKing Oyster, Eryngii

JournalPeptides

Year2004

Key points

A ribonuclease with a temperature optimum of about 70 degrees C and a pH optimum of 6.5 was isolated from fruiting bodies of the mushroom Pleurotus eryngii
The ribonuclease was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and S-Sepharose
It possessed a molecular mass of 16 kDa, and exhibited higher ribonucleolytic activity toward poly A and poly G and lower ribonucleolytic activity toward poly C and poly U. Its N-terminal sequence was distinctly different from those of other mushroom ribonucleases, and resembled that of Pleurotus tuber-regium only by 40%
Furthermore, its thermostability characteristics, polyhomoribonucleotide specificity and molecular mass were dissimilar to those of other mushroom ribonucleases

Metadata-grounded summary

Citation abstract

A ribonuclease with a temperature optimum of about 70 degrees C and a pH optimum of 6.5 was isolated from fruiting bodies of the mushroom Pleurotus eryngii. The ribonuclease was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and S-Sepharose. It possessed a molecular mass of 16 kDa, and exhibited higher ribonucleolytic activity toward poly A and poly G and lower ribonucleolytic activity toward poly C and poly U. Its N-terminal sequence was distinctly different from those of other mushroom ribonucleases, and resembled that of Pleurotus tuber-regium only by 40%. Furthermore, its thermostability characteristics, polyhomoribonucleotide specificity and molecular mass were dissimilar to those of other mushroom ribonucleases.

Citation

Ng TB, Wang HX (2004). A novel ribonuclease from fruiting bodies of the common edible mushroom Pleurotus eryngii. Peptides https://doi.org/10.1016/j.peptides.2004.01.027 PMID: 15350705

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