Results 11 to 20 of about 92,781 (236)

Auxin-induced WRKY23 activates PECTIN LYASE-LIKE1 and PECTIN LYASE-LIKE3 for apoplastic iron reutilization in Arabidopsis roots

open access: yesPlant Stress
The retention and reutilization of apoplastic iron (Fe) are essential for Fe homeostasis in plants, yet the underlying molecular mechanisms remain largely unexplored. Here, we characterized the role of WRKY23, a nucleus-localized transcription factor, in
Yuzhen Zhang   +6 more
doaj   +3 more sources

Purification and some properties of the pectin lyase fromPenicillium italicum [PDF]

open access: yesFEBS Letters, 1991
For the first time, a pectin lyase (poly(methoxygalacturonide)lyase; EC 4.2.2.10) from a member of the generus Penicillium was isolated, purified to homogeneity and characterized. The monomeric enzyme from Penicillium italicum CECT 2294 culture filtrates
Maria J Llama   +2 more
exaly   +4 more sources

The pectin lyases in Arabidopsis thaliana: evolution, selection and expression profiles. [PDF]

open access: yesPLoS ONE, 2012
Pectin lyases are a group of enzymes that are thought to contribute to many biological processes, such as the degradation of pectin. However, until this study, no comprehensive study incorporating phylogeny, chromosomal location, gene duplication, gene ...
Jun Cao
doaj   +4 more sources

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755. [PDF]

open access: yes3 Biotech, 2017
Using solid-state fermentation, production of an industrially important pectin lyase from a fungal strain Fusarium oxysporum MTCC 1755 was attempted, which was further subjected to purification and characterization. The enzyme was purified by three steps,
Yadav S   +4 more
europepmc   +2 more sources

Safety evaluation of the food enzyme pectin lyase from the non‐genetically modified Aspergillus luchuensis strain LC‐07 [PDF]

open access: yesEFSA Journal
The food enzyme pectin lyase (1,4‐6‐O‐methyl‐α‐D‐galacturonan lyase; EC 4.2.2.10) is produced with the non‐genetically modified Aspergillus luchuensis strain LC‐07 by Shin Nihon Chemical Co., Ltd.
EFSA Panel on Food Enzymes (FEZ)   +17 more
doaj   +2 more sources

GS-E3D, a new pectin lyase-modified red ginseng extract, inhibited diabetes-related renal dysfunction in streptozotocin-induced diabetic rats. [PDF]

open access: yesBMC Complement Altern Med, 2017
BackgroundGS-E3D is a newly developed pectin lyase-modified red ginseng extract. The purpose of this study was to investigate the therapeutic effects of GS-E3D on diabetes-related renal dysfunction in streptozotocin-induced diabetic rats.MethodGS-E3D (25,
Kim CS, Jo K, Kim JS, Pyo MK, Kim J.
europepmc   +2 more sources

Optimizing pectin lyase production using the one‐factor‐at‐a‐time method and response surface methodology

open access: yesBiotechnology and applied biochemistry
Pectinases are commonly industrially synthesized by molds. This study aimed to optimize pectin lyase synthesis by a bacterium, Pseudomonas fluorescens, using both the one‐factor‐at‐a‐time (OFAT) method and response surface methodology.
Ertuğrul Gül   +4 more
semanticscholar   +2 more sources

Resolving Isomeric Structures in Natural Complex Carbohydrates: A Comparative Study of SLIM and Cyclic Ion Mobility Platforms. [PDF]

open access: yesRapid Commun Mass Spectrom
ABSTRACT Rationale Recent advances in ion mobility mass spectrometry (IMS) have led to the development of high‐resolution platforms such as cyclic IMS and SLIM IMS (structures for lossless ion manipulations), both offering enhanced capabilities for resolving complex biomolecular conformations.
Benazza R   +5 more
europepmc   +2 more sources

Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases

open access: yesStructure, 1997
Background: Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall. The homogalacturan backbone of pectin varies in its degree of methylation from the highly methylated and relatively ...
Olga Mayans   +2 more
exaly   +2 more sources

Purification and Characterization of a Unique Pectin Lyase from Aspergillus giganteus Able to Release Unsaturated Monogalacturonate during Pectin Degradation [PDF]

open access: yesEnzyme Research, 2014
A pectin lyase, named PLIII, was purified to homogeneity from the culture filtrate of Aspergillus giganteus grown in submerged culture containing orange peel waste as carbon source.
D. Pedrolli, E. C. Carmona
semanticscholar   +2 more sources

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