Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata

Geng, Xiao; Te, Rigen; Gao, Tian; Zhao, Yongchang; Zhao, Liyan; Wang, Hexiang; Ng, Tzi Bun

doi:10.18388/abp.2016_1431

Cited by 4 publications

(2 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some proteases from edible mushroom are listed in Table IV. Metalloprotease from Oudemansiella radicata was purified from the mushroom extract through DEAE-cellulose column equilibrated with sodium acetate buffer at pH5.6 (Geng & Ng, 2017). The pure enzyme was characterized for its activator, inhibitors, Km, Vax, temp and pH optima etc.…”

Section: ) Proteasementioning

confidence: 99%

Edible Mushroom: A Potent Producer of Industrial Enzymes

Ghorai¹

2022

JSR

View full text Add to dashboard Cite

Edible mushrooms are hugely appreciated in every part of the world because of their nutritive value, ease of production as well as non-toxicity. In recent years we are getting more inquisitive about these culinary wonders as they are showcasing a wide array of secondary metabolites with numerous potential applications. These nutritionally rich food supplements are capable of producing a number of enzymes having prospects in industries like brewery, dairy, food & feed processing, textile, paper, leather, agrochemical, photography and pharmaceuticals etc. This article reviews quite a few of the reported enzymes available from wild and cultured edible mushrooms for their production media, production rates and functional attributes. Recent reports of parameters affecting their production are noted as well. The article has also discussed application prospects and current omics approaches exploring intricate roles of mushroom enzymes in development and metabolic pathways of these edible fruiting bodies. Cumulative treatment makes this article one uniquely up-to-date and comprehensive narrative of edible mushroom enzymes.

show abstract

Section: ) Proteasementioning

confidence: 99%

Edible Mushroom: A Potent Producer of Industrial Enzymes

Ghorai¹

2022

JSR

View full text Add to dashboard Cite

show abstract

“…The marked suppression of the protease activity by EDTA indicates that the protease is a metalloprotease. 52…”

Section: © Author(s)mentioning

confidence: 99%

Diethylaminoethyl cellulose (DEAE-C) between chromatography and synthetic applications

Aljaf¹,

Amin²,

Hussain³

et al. 2020

Arkivoc

View full text Add to dashboard Cite

The aim of this review is to point out the attention of the reader to the use of DEAE-C in organic reactions, possibly not only devoted to the preparation of heterocycles but potentially extending to other classes of organic compounds. Being DEAE-C an ammonium salt commonly used in chromatographic applications, it can be considered as a potential mild acid catalyst or a proton donor and these features can in theory catalyze standard acid-catalyzed organic reactions. In addition, the resin nature of DEAE-C could suggest the way to perform organic reactions in the solid state.

show abstract

Purification, Characterization, and Immobilization of a Novel Protease-Resistant α-Galactosidase from Oudemansiella radicata and Its Application in Degradation of Raffinose Family Oligosaccharides from Soymilk

Geng

Lei

Bau

et al. 2022

Foods

View full text Add to dashboard Cite

α-galactosidase (EC 3.2.1.22) are glycosidases that catalyze the hydrolysis of α-1,6-linked D-galactosyl residues of different substrates, which has been widely applied in the food industry. Oudemansiella radicata is a kind of precious edible medicinal mushroom, which is a healthy, green, and safe food-derived enzyme source. In this study, a novel acidic α-galactosidase was purified from the dry fruiting bodies of O. radicata by ion-exchange chromatography and gel filtration, and designated as ORG (O. radicata α-galactosidase). ORG was further immobilized to obtain iORG by the sodium alginate–chitosan co-immobilization method. Then, the characterization of free and immobilized enzymes and their potential application in the removal of the RFOs from soymilk were investigated. The results showed that ORG might be a 74 kDa heterodimer, and it exhibited maximum activity at 50 °C and pH 3.0, whereas iORG showed maximum activity at 50 °C and pH 5.5. In addition, iORG exhibited higher thermal stability, pH stability, storage stability, and a better degradation effect on raffinose family oligosaccharides (RFOs) in soymilk than ORG, and iORG completely hydrolyzed RFOs in soymilk at 50 °C within 3 h. Therefore, iORG might be a promising candidate in the food industry due to its excellent stability, high removal efficiency of RFOs from soymilk, and great reusability.

show abstract

Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata

Cited by 4 publications

References 48 publications

Edible Mushroom: A Potent Producer of Industrial Enzymes

Edible Mushroom: A Potent Producer of Industrial Enzymes

Diethylaminoethyl cellulose (DEAE-C) between chromatography and synthetic applications

Purification, Characterization, and Immobilization of a Novel Protease-Resistant α-Galactosidase from Oudemansiella radicata and Its Application in Degradation of Raffinose Family Oligosaccharides from Soymilk

Contact Info

Product

Resources

About