l asparagine/kartupelis

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Effective treatment for suppression of acrylamide formation in fried potato chips using L-asparaginase from Bacillus subtilis.

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It has been reported that acrylamide, a potential carcinogen, is formed from the reaction of L-asparagine (L-Asn) and reducing sugars contained in foods during heating processes and free asparagine is a limiting factor for acrylamide formation. It has been reported that potato products such as

Reduction of acrylamide formation by vanadium salt in potato French fries and chips.

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The effects of vanadyl sulphate on the formation of acrylamide have been studied in fried potato products, such as French fries and chips. Acrylamide formation was inhibited by 30.3%, 53.3% and 89.3% when the sliced potato strips were soaked in 0.001, 0.01 and 0.1 M vanadyl sulphate (VOSO(4))

Biochemical characterization of a novel L-asparaginase from Paenibacillus barengoltzii being suitable for acrylamide reduction in potato chips and mooncakes.

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A novel L-asparaginase gene (PbAsnase) from Paenibaeillus barengoltzii CAU904 was cloned and expressed in Escherichia coli. The L-asparaginase gene was 1011bp encoding 336 amino acids. Multiple sequence alignment of PbAsnase with other known L-asparaginases revealed that the enzyme showed high

Characterization of a novel type I l-asparaginase from Acinetobacter soli and its ability to inhibit acrylamide formation in potato chips.

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l-Asparaginases have the potential to inhibit the formation of acrylamide, a harmful toxin formed during high temperature processing of food. A novel bacterium which produces l-asparaginase was screened. Type I l-asparaginase gene from Acinetobacter soli was cloned and expressed in Escherichia coli.

Molecular cloning, structural modeling and characterization of a novel glutaminase-free L-asparaginase from Cobetia amphilecti AMI6.

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The exploration of new sources of L-asparaginase with low glutaminase activity is of great interest in both medical and food applications. In the current study, a novel L-asparaginase gene (CobAsnase) from halotolerant Cobetia amphilecti AMI6 was cloned and over-expressed in Escherichia coli. The

Cloning, expression, and characterization of L-asparaginase from a newly isolated Bacillus subtilis B11-06.

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This study focused on the cloning, overexpression, and characterization of the gene encoding L-asparaginase (ansZ) from a nonpathogenic strain of Bacillus subtilis B11-06. The recombinant enzyme showed high thermostability and low affinity to L-glutamine. The ansZ gene, encoding a putative

Vegetative Compatibility Groups of Fusarium oxysporum f. sp. cepae from Onion in Colorado.

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Nineteen isolates of Fusarium oxysporum f. sp. cepae recovered from diseased onions growing in the western, southern, and northern regions of Colorado were placed into vegetative compatibility groups (VCGs) based on pairing of complementary mutants. Pathogenic isolates from these regions were

Optimization of aqueous two-phase micellar system for partial purification of L-asparaginase from Penicillium sp. grown in wheat bran as agro-industrial residue

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L-asparaginase has been used in the remission of malignant neoplasms such as acute lymphoblastic leukemia. The search for new sources of this enzyme has become attractive for therapeutics. Traditional methods for biomolecule purification involve several steps. A two-phase system may be a good

Reduction of acrylamide level through blanching with treatment by an extremely thermostable L-asparaginase during French fries processing.

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Bacterial L-asparaginase catalyzes the hydrolysis of L-asparagine to L-aspartic acid. It is normally used as an antineoplastic drug applied in lymphoblastic leukemia chemotherapy and as a food processing aid in baked or fried food industry to inhibit the formation of acrylamide. The present study

Xylella fastidiosa cultivation on a minimal solid defined medium.

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A simple defined solid medium containing citrate and succinate, three amino acids (L-glutamine, L-asparagine, and L-cysteine), hemin chloride, potato starch, gellan gum (GelRite), and mineral salts supported the growth of grape strains of Xylella fastidiosa, the bacterial pathogen that causes

Catalytic characteristics and application of l-asparaginase immobilized on aluminum oxide pellets.

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l-asparaginase from Escherichia coli (l-ASNase) was covalently immobilized on aluminum oxide pellets (AlOPs) using a cross-linking agent, glutaraldehyde. Maximum immobilization yield (85.0%) was obtained after optimizing immobilization parameters using response surface methodology (RSM). Both free

Angular Leaf Spot of Cucumber Caused by Pseudomonas syringae pv. lachrymans in Kurdistan.

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During the spring of 2004 and 2005, angular leaf spot was observed on cucumber (Cucumis sativus L.) in some areas of Kurdistan Province in Iran for the first time. Disease incidence in affected fields was approximately 100%. Symptoms were initially small, round or irregular, water-soaked spots on

First Report of Bacterial Leaf Blight of Coriander Caused by Xanthomonas campestris pv. coriandri in Taiwan.

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Leaf blight symptoms on coriander (Coriandrum sativum) were observed during the summers of 2000 to 2002 in fields at the Beidou and Sijhou townships, Changhua County, Taiwan. Symptoms first appeared as small spots on the lower sides of leaves and stems. The centers of the spots quickly turned brown

Purification, characterization and kinetic properties of extracellular L-asparaginase produced by Cladosporium sp.

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L-asparaginase from Cladosporium sp. grown on wheat bran by SSF was purified. Enzyme appeared to be a trimer with homodimer of 37 kDa and another 47 kDa amounting to total mass of 121 kDa as estimated by SDS-PAGE and 120 kDa on gel filtration column. The optimum temperature and pH of the enzyme were

A novel bacterial type II l-asparaginase and evaluation of its enzymatic acrylamide reduction in French fries.

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This study reports the identification of a novel bacterial type II l-asparaginase, abASNase2, from Aquabacterium sp. A7-Y. The enzyme contains 319 amino acids and shared 35% identity with Escherichia coli type II l-asparaginase (EcAII), a commercial enzyme trademarked Elspar® that is widely used for

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