نتایج جستجو برای: pectin lyase enzyme

تعداد نتایج: 252689  

Journal: :پژوهش های علوم و صنایع غذایی ایران 0
s.m. dadpour m. khomeiri h.r. sadeghi pour sh. rofigari haghighat m. aalami

fermentation is an important process for black tea production. during this process, by exposure of substrate to enzymes and the underlying oxidation reactions, quality determining factors of tea is produced. it is known that the exogenous application of cell-wall degrading enzymes leads to the increased production of these compounds through enhancement of enzyme-substrate interactions. pectinas...

Journal: :Microbial Cell Factories 2005
Rigini M Papi Sotiria A Chaitidou Fotini A Trikka Dimitrios A Kyriakidis

BACKGROUND Production of heterologous proteins in the E. coli periplasm, or into the extracellular fluid has many advantages; therefore naturally occurring signal peptides are selected for proteins translocation. The aim of this study was the production in high yields of a recombinant pectin lyase that is efficiently secreted and the encapsulation of transformed E. coli cells for pectin degrada...

Journal: :Applied and environmental microbiology 1981
B Schink J C Ward J G Zeikus

Wetwood samples from standing trees of eastern cottonwood (Populus deltoides), black poplar (Populus nigra), and American elm (Ulmus americana) contained high numbers of aerobic and anaerobic pectin-degrading bacteria (10 to 10 cells per g of wood). High activity of polygalacturonate lyase (</=0.5 U/ml) was also detected in the fetid liquid that spurted from wetwood zones in the lower trunk whe...

2009
Aurora Martínez-Trujillo Juan S. Aranda Carlos Gómez-Sánchez Blanca Trejo-Aguilar Guillermo Aguilar-Osorio

Growth and enzymes production by Aspergillus flavipes FP-500 were evaluated on pectin, polygalacturonic acid, galacturonic acid, arabinose, rhamnose, xylose, glycerol and glucose at different initial pH values. We found that the strain produced exopectinases, endopectinases and pectin lyases. Exopectinases and pectin lyase were found to be produced at basal levels as constitutive enzymes and th...

2002
A. F. AFIFI

Utilization of orange peels as an agroindustrial waste for production of pectin lyase (PL) [E.C.4.2.2.10] by Curvularia inaequalis (Shear) Boedijn NRRL 13884 was investigated using solid state culture (SSC). The highest level of extracellular pectin lyase was detected with this waste as an inducing substrate. The enzyme was purified using Sephadex G-100 and DEAE-Cellulose column chromatography....

2013
Keith R. Davis Alan G. Darvill Peter Albersheim Anne Dell

Endopolygalacturonic acid lyase, purified from the phytopathogenic bacterium, Erwinia carotovora , induces phytoalexin accumulation in soybean ( Glycine max L .) cotyledons. This pectin-degrading enzyme releases heat-stable elicitors of phytoalexin accumulation from soybean cell walls, citrus pectin, and citrus sodium polypectate. The most elicitor-active m olecules ob­ tained by treating soybe...

2014
Danielle Biscaro Pedrolli Eleonora Cano Carmona

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. PLIII was able to digest apple pectin and citrus pectins with different degrees of methyl esterification. Interestingly, the PLIII activity was stimulated in the presence of some divalent cations including Pb(2+) an...

Journal: :Journal of the agricultural chemical society of Japan 1988

Background: Pectinases are pectin degrading class of enzymes including polygalacturonase (PG), polymethyl galacturonase (PMG), pectate lyase (PEL), and pectin esterase (PE) that are commonly used in processes involving the degradation of plant materials, such as speeding up the extraction of fruit juices. Objectives: A highly methylated pectin degrading bacterium from soil covered with fruit wa...

Journal: :Bioscience, biotechnology, and biochemistry 2005
Si Si Hla Junji Kurokawa Suryani Tetsuya Kimura Kunio Ohmiya Kazuo Sakka

The Clostridium stercorarium F-9 pel9A gene encodes a pectate lyase Pel9A consisting of 1,240 amino acids with a molecular weight of 135,171. The mature form of Pel9A is a modular enzyme composed of two family-9 catalytic modules of polysaccharide lyases, CM9-1 and CM9-2, in order from the N terminus. Pel9A showed an overall sequence similarity to the hypothetical pectate lyase PelX of Bacillus...

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