Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica

2001 ◽  
Vol 47 (9) ◽  
pp. 861-870 ◽  
Author(s):  
Pascale Jolivet ◽  
Edith Bergeron ◽  
Haguith Benyair ◽  
Jean-Claude Meunier
Keyword(s):  
Acid Phosphatase ◽  
Yarrowia Lipolytica ◽  
Protein Phosphatase ◽  
Protein Phosphatases ◽  
Major Protein ◽  
Ethanol Treatment ◽  
Early Stationary Phase ◽  
Yeast Strains ◽  
Deficient Medium

Casein phosphatase activities have been identified in five yeast strains grown on Pi-deficient medium. Maximal endocellular activities appeared in the exponential phase. Exocellular phosphatases were significantly produced from Yarrowia lipolytica W-29 and Kluyveromyces marxianus, in the early stationary phase. Major phosphatases from K. marxianus were one heavy acid phosphatase composed of 64–67 kDa subunits, which could be secreted in the medium, and one type 2A protein phosphatase with an apparent molecular mass of 147 kDa and a 52 kDa catalytic subunit dissociated by 80% ethanol treatment. The characteristics of phosphatases purified from K. marxianus were compared with those previously purified from Y. lipolytica.Key words: yeast, type 2A protein phosphatase, acid phosphatase, [32P]casein, Pi deficiency.

Purification and characterization of a type 2A protein phosphatase from Yarrowia lipolytica grown on a phosphate-deficient medium

1997 ◽  
Vol 320 (6) ◽  
pp. 441-449 ◽  
Author(s):  
Pascale Jolivet ◽  
Claudine Queiroz-Claret ◽  
Édith Bergeron ◽  
Jean-Claude Meunier
Keyword(s):  
Yarrowia Lipolytica ◽  
Protein Phosphatase ◽  
Purification And Characterization ◽  
Deficient Medium

Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica

2001 ◽  
Vol 47 (9) ◽  
pp. 861-870 ◽  
Author(s):  
Pascale Jolivet ◽  
Edith Bergeron ◽  
Haguith Benyair ◽  
Jean-Claude Meunier
Keyword(s):  
Yarrowia Lipolytica ◽  
Protein Phosphatases ◽  
Major Protein

Isolation and characterization of two crude oil-degrading yeast strains, Yarrowia lipolytica PG-20 and PG-32, from the Persian Gulf

2012 ◽  
Vol 64 (7) ◽  
pp. 1386-1391 ◽  
Author(s):  
Mehdi Hassanshahian ◽  
Hamid Tebyanian ◽  
Simone Cappello
Keyword(s):  
Crude Oil ◽  
Yarrowia Lipolytica ◽  
Persian Gulf ◽  
Isolation And Characterization ◽  
Yeast Strains ◽  
The Persian Gulf

scholarly journals Purification and characterization of two wheat-embryo protein phosphatases

1988 ◽  
Vol 251 (2) ◽  
pp. 357-363 ◽  
Author(s):  
G M Polya ◽  
M Haritou
Keyword(s):  
Protein Phosphatase ◽  
Wheat Germ ◽  
Protein Phosphatases ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Dependent Protein Kinase ◽  
Wheat Embryo ◽  
Dependent Protein ◽  
Enzyme I

Two protein phosphatases (enzymes I and II) were extensively purified from wheat embryo by a procedure involving chromatography on DEAE-cellulose, phenyl-Sepharose CL-4B, DEAE-Sephacel and Ultrogel AcA 44. Preparations of enzyme I (Mr 197,000) are heterogeneous. Preparations of enzyme II (Mr 35,000) contain only one major polypeptide (Mr 17,500), which exactly co-purifies with protein phosphatase II on gel filtration and is not present in preparations of enzyme I. However, this major polypeptide has been identified as calmodulin. Calmodulin and protein phosphatase II can be separated by further chromatography on phenyl-Sepharose CL-4B. Protein phosphatases I and II do not require Mg2+ or Ca2+ for activity. Both enzymes catalyse the dephosphorylation of phosphohistone H1 (phosphorylated by wheat-germ Ca2+-dependent protein kinase) and of phosphocasein (phosphorylated by wheat-germ Ca2+-independent casein kinase), but neither enzyme dephosphorylates a range of non-protein phosphomonoesters tested. Both enzymes are inhibited by Zn2+, Hg2+, vanadate, molybdate, F-, pyrophosphate and ATP.

Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity

Biochemistry ◽  
1988 ◽  
Vol 27 (12) ◽  
pp. 4265-4273 ◽  
Author(s):  
Abdul Waheed ◽  
Piotr M. Laidler ◽  
Yu Yuan P. Wo ◽  
Robert L. Van Etten
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Physicochemical Characterization

Characterization of an exocellular protein phosphatase with dual substrate specificity from the yeast Yarrowia lipolytica

1998 ◽  
Vol 30 (7) ◽  
pp. 783-796 ◽  
Author(s):  
Pascale Jolivet ◽  
Claudine Queiroz-Claret ◽  
Edith Bergeron ◽  
Jean-Claude Meunier
Keyword(s):  
Substrate Specificity ◽  
Yarrowia Lipolytica ◽  
Protein Phosphatase ◽  
Dual Substrate Specificity ◽  
Yeast Yarrowia Lipolytica ◽  
Dual Substrate

Taxonomic characterization and identification of Saccharomyces cerevisiae D8 for brandy production from pineapple

2018 ◽  
Vol 39 (4) ◽  
pp. 474-482
Author(s):  
Hoang Thi Le Thuong ◽  
Nguyen Quang Hao ◽  
Tran Thi Thuy
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Low Ph ◽  
Yeast Strains ◽  
Biological Studies ◽  
Taxonomic Characterization

Eight yeast strains (denoted as D1 to D8) were isolated from samples of natural fermented pineapple. Strain D8 showed highest alcoholic production at low pH and special aroma of pineapple has been chosen for further study. Taxonomic characterization of strain D8 using morphological, biochemical and molecular biological studies confirmed that strain D8  belong to Saccharomycetaceae family, Saccharomycetales order and Saccharomyces cerevisiae species. Therefore, we named this strain as Saccharomyces cerevisiae D8 for further study on Brandy production from pineapple. Citation: Hoang Thi Le Thuong, Nguyen Quang Hao, Tran Thi Thuy, 2017. Taxonomic characterization and identification of Saccharomyces cerevisiae D8 for brandy production from pineapple. Tap chi Sinh hoc, 39(4): 474- 482. DOI: 10.15625/0866-7160/v39n4.10864.*Corresponding author: [email protected] Received 5 December 2016, accepted 12 August 2017

Purification and characterization of the catalytic subunit of protein phosphatase 1 from Neurospora crassa

1997 ◽  
Vol 48 (3) ◽  
pp. 289-302 ◽  
Author(s):  
B. Szöőr ◽  
V. Dombrádi ◽  
P. Gergely ◽  
Z. Fehér
Keyword(s):  
Neurospora Crassa ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Purification And Characterization
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