نتایج جستجو برای: pichia pastoris gs115

تعداد نتایج: 4312  

2014
Hanpeng Liao Shuixian Li Haiping Zheng Zhong Wei Dongyang Liu Waseem Raza Qirong Shen Yangchun Xu

BACKGROUND Endo-1,4-β-mannanase is an enzyme that can catalyze the random hydrolysis of β-1, 4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans and has a number of applications in different biotechnology industries. Penicillium oxalicum is a powerful hemicellulase-producing fungus (Bioresour Technol 123:117-124, 2012); however, few previous studies have focused ...

Journal: :Cellular and Molecular Biology Letters 2006

2012

The yeast pichia pastoris is widely used as host for heterologous protein expression for hundreds of different proteins. Recently, the organism has received attention in the biologics industry when the first pichia-derived biopharmaceutical protein received market approval by the FDa. pichia expression cells can furnish yields of more than 10 g/L of secreted recombinant target protein. However,...

2012
Ana Leticia Vanz Heinrich Lünsdorf Ahmad Adnan Manfred Nimtz Chandrasekhar Gurramkonda Navin Khanna Ursula Rinas

BACKGROUND Pichia pastoris is an established eukaryotic host for the production of recombinant proteins. Most often, protein production is under the control of the strong methanol-inducible aox1 promoter. However, detailed information about the physiological alterations in P. pastoris accompanying the shift from growth on glycerol to methanol-induced protein production under industrial relevant...

Journal: :Current opinion in structural biology 2015
Bernadette Byrne

The methylotrophic yeast Pichia pastoris is a widely used recombinant expression host. P. pastoris combines the advantages of ease of use, relatively rapid expression times and low cost with eukaryotic co-translational and post-translational processing systems and lipid composition. The suitability of P. pastoris for high density controlled culture in bioreactors means large amounts of protein ...

2013
Daniel Weinacker Claudia Rabert Andrea B. Zepeda Carolina A. Figueroa Adalberto Pessoa Jorge G. Farías

Since the 1970s, the establishment and development of the biotech industry has improved exponentially, allowing the commercial production of biopharmaceutical proteins. Nowadays, new recombinant protein production is considered a multibillion-dollar market, in which about 25% of commercial pharmaceuticals are biopharmaceuticals. But to achieve a competitive production process is not an easy tas...

2017
Saeed Azadi Arash Mahboubi Nasser Naghdi Roya Solaimanian Seyyed Alireza Mortazavi

Recombinant protein production in Pichia pastoris is based on alcohol oxidase promoters which are regulated by methanol. However, the use of methanol has several disadvantages, which is why current trends in bioprocess development with Pichia pastoris (P. pastoris) are focusing on methanol mixed feeding strategies. This work aimed to develop a new experimental method and compare the effect of v...

Hosnieh Ghasemi, Mahsa Nayebhashemi, Monire Jamalkhah, Mozhgan Zahmatkesh, Nafiseh Moeinian, Najmeh Zarei, Somayeh Enayati, Vahid Khalaj, Zahra Mohammadi,

Background: The methylotrophic yeast Pichia pastoris is an appealing production host for a variety of recombinant, including biologics. In this sense, various genetic- and non-genetic-based techniques have been implemented to improve the production efficiency of this expression platform. Los1 (loss of supression) encodes a non-essential nuclear tRNA exporter in Saccharomyces cerevisiae, which i...

Journal: :Autophagy 2007
Jean-Claude Farré Jason Vidal Suresh Subramani

The cytoplasm-to-vacuole targeting (Cvt) pathway of Saccharomyces cerevisiae delivers aminopeptidase I (Ape1) from the cytosol to the vacuole, bypassing the normal secretory route. The Cvt pathway, although well-studied, was known only in S. cerevisiae. We demonstrate its existence in the methylotrophic yeast, Pichia pastoris, where it also delivers P. pastoris Ape1 (PpApe1) to the vacuole. Mos...

Laccase (EC 1.10.3.2) are multi-copper oxidase which catalyze the oxidation aromatic and non- aromatic compounds with electron reduction of molecular oxygen to water. Nucleotide sequence of laccase (accession number : ) was optimized according codon preference of Pichia pastoris. Gene was synthesized and cloned into pPICZalpha A. laccase under control of AOX1 promoter was transformed to P.pasto...

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