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Cloning and heterologous expression of a hydrophobin gene Ltr. hyd from the tiger milk mushroom Lentinus tuber-regium in yeast-like cells of Tremella fuciformis
Liu, Dongmei; Zhu, Hanyu; Chen, Yue; Zheng, Liesheng; Chen, Liguo; Ma, Aimin.
  • Liu, Dongmei; Huazhong Agricultural University. College of Food Science and Technology. Wuhan. CN
  • Zhu, Hanyu; Huazhong Agricultural University. College of Food Science and Technology. Wuhan. CN
  • Chen, Yue; Huazhong Agricultural University. College of Food Science and Technology. Wuhan. CN
  • Zheng, Liesheng; Huazhong Agricultural University. College of Plant Science and Technology. Wuhan. CN
  • Chen, Liguo; Huazhong Agricultural University. College of Plant Science and Technology. Wuhan. CN
  • Ma, Aimin; Huazhong Agricultural University. College of Food Science and Technology. Wuhan. CN
Electron. j. biotechnol ; 32: 6-12, Mar. 2018. tab, graf, ilus
Article in English | LILACS | ID: biblio-1022493
ABSTRACT

Background:

Hydrophobins are small proteins secreted by filamentous fungi, which show a highly surface activity. Because of the signally self-assembling abilities and surface activities, hydrophobins were considered as candidates in many aspects, for example, stabilizing foams and emulsions in food products. Lentinus tuber-regium, known as tiger milk mushroom, is both an edible and medicinal sclerotium-producing mushroom. Up to now, the hydrophobins of L. tuber-regium have not been identified.

Results:

In this paper, a Class I hydrophobin gene, Ltr.hyd, was cloned from L. tuber-regium and expressed in the yeast-like cells of Tremella fuciformis mediated by Agrobacterium tumefaciens. The expression vector pGEH-GH was under the control of T. fuciformis glyceraldehyde-3-phosphate dehydrogenase gene (gpd) promoter. The integration of Ltr.hyd into the genome of T. fuciformis was confirmed by PCR, Southern blot, fluorescence observation and quantitative real-time PCR (qRT-PCR). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that recombinant hydrophobin rLtr.HYD with an expected molecular mass of 13 kDa was extracted. The yield of rLtr.HYD was 0.66 mg/g dry weight. The emulsifying activity of rLtr.HYD was better than the typical food emulsifiers sodium caseinate and Tween 20.

Conclusions:

We evaluated the emulsifying property of hydrophobin Ltr.HYD, which can be potentially used as a food emulsifier.
Subject(s)


Full text: Available Index: LILACS (Americas) Main subject: Basidiomycota / Fungal Proteins / Lentinula Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2018 Type: Article / Project document Affiliation country: China Institution/Affiliation country: Huazhong Agricultural University/CN

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Full text: Available Index: LILACS (Americas) Main subject: Basidiomycota / Fungal Proteins / Lentinula Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2018 Type: Article / Project document Affiliation country: China Institution/Affiliation country: Huazhong Agricultural University/CN