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beta glucosidase/ryža siata

Odkaz sa uloží do schránky
ČlánkyKlinické štúdiePatenty
Strana 1 od 21 výsledky

Hydrolysis of Conjugated Gibberellins by β-Glucosidases from Dwarf Rice (Oryza sativa L. cv. «Tan-ginbozu»).

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Dwarf rice (Oryza sativa L. cv. «Tan-ginbozu») is widely used for gibberellin conjugate bioassay. Soluble and particulate fractions from seeds and seedlings of this variety showed hydrolytic activity toward [(3)H]GA-O-Glc. The soluble fraction from mature seeds exhibited the highest

Expression and enzymatic properties of rice (Oryza sativa L.) monolignol β-glucosidases.

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Monolignol glucosides and their β-glucosidases are found in monocots, but their biological roles are unclear. Phylogenetic analysis of rice (Oryza sativa L.) glycoside hydrolase family GH1 β-glucosidases indicated that Os4BGlu14, Os4BGlu16, and Os4BGlu18 are closely related to known monolignol

Expression, purification, crystallization and preliminary X-ray analysis of rice (Oryza sativa L.) Os4BGlu12 beta-glucosidase.

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Rice (Oryza sativa L.) Os4BGlu12, a glycoside hydrolase family 1 beta-glucosidase (EC 3.2.1.21), was expressed as a fusion protein with an N-terminal thioredoxin/His(6) tag in Escherichia coli strain Origami B (DE3) and purified with subsequent removal of the N-terminal tag. Native Os4BGlu12 and its
GH5BG, the cDNA for a stress-induced GH5 (glycosyl hydrolase family 5) beta-glucosidase, was cloned from rice (Oryza sativa L.) seedlings. The GH5BG cDNA encodes a 510-amino-acid precursor protein that comprises 19 amino acids of prepeptide and 491 amino acids of mature protein. The protein was
Rice Os4BGlu12, a glycoside hydrolase family 1 (GH1) β-glucosidase, hydrolyzes β-(1,4)-linked oligosaccharides of 3-6 glucosyl residues and the β-(1,3)-linked disaccharide laminaribiose, as well as certain glycosides. The crystal structures of apo Os4BGlu12, and its complexes with

Identification of a beta-glucosidase hydrolyzing tuberonic acid glucoside in rice (Oryza sativa L.).

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Tuberonic acid (TA) and its glucoside (TAG) have been isolated from potato (Solanum tuberosum L.) leaflets and shown to exhibit tuber-inducing properties. These compounds were reported to be biosynthesized from jasmonic acid (JA) by hydroxylation and subsequent glycosylation, and to be contained in
β-glucosidase is an enzyme that has ability to cleave β-glycosidic bonds present in oligosaccharides and glycoconjugates. They are known to be present across all domains of living organism and have important roles in many biological processes including plant defense mechanism. In the present study,

Identification of rice β-glucosidase with high hydrolytic activity towards salicylic acid β-D-glucoside.

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β-Glucosidases (EC 3.2.1.21) split β-glucosidic linkages at the non-reducing end of glucosides and oligosaccharides to release β-D-glucose. One of the important functions of plant β-glucosidase is deglucosylation of inactive glucosides of phytohormones to regulate levels of active hormones.

Cloning and characterization of drought responsive partial gene sequence(s) from Oryza sativa L. subsp. Indica.

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Differential display gels were run for the drought tolerant (N-22) and drought susceptible (Panidhan) genotypes of rice (Oryza sativa) to identify the genes showing differential expression with respect to moisture stress. Differential cDNA products were cloned in PCR-Trap vector and analyzed for
Rice (Oryza sativa) BGlu1 beta-glucosidase was expressed in Escherichia coli with N-terminal thioredoxin and hexahistidine tags and purified by immobilized metal-affinity chromatography (IMAC). After removal of the N-terminal tags, cation-exchange and S-200 gel-filtration chromatography yielded a 50

Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu1.

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The bglu1 cDNA for a beta-glucosidase cloned from rice (Oryza sativa L.) seedlings was expressed as a soluble and active protein in Escherichia coli and designated BGlu1. This enzyme hydrolysed beta-1,4-linked oligosaccharides with increasing catalytic efficiency (kcat/Km) values as the DP (degree
Glycoside hydrolase family 1 (GH1) beta-glucosidases play roles in many processes in plants, such as chemical defense, alkaloid metabolism, hydrolysis of cell wall-derived oligosaccharides, phytohormone regulation, and lignification. However, the functions of most of the 34 GH1 gene products in rice

Increase phosphorus availability from the use of alfalfa (Medicago sativa L) green manure in rice (Oryza sativa L.) agroecosystem.

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Alfalfa is a good green manure source, but its effect on rice growth has not been fully elucidated. Two green manure species, alfalfa and broad bean (Vicia faba L.), and two N fertilizer levels, alone or combination, were applied to a rice field. The results indicated that alfalfa had more

Effects of winter cover crops residue returning on soil enzyme activities and soil microbial community in double-cropping rice fields.

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Residue management in cropping systems is useful to improve soil quality. However, the studies on the effects of residue management on the enzyme activities and microbial community of soils in South China are few. Therefore, the effects of incorporating winter cover crop residue with a

Rice Os9BGlu31 is a transglucosidase with the capacity to equilibrate phenylpropanoid, flavonoid, and phytohormone glycoconjugates.

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Glycosylation is an important mechanism of controlling the reactivities and bioactivities of plant secondary metabolites and phytohormones. Rice (Oryza sativa) Os9BGlu31 is a glycoside hydrolase family GH1 transglycosidase that acts to transfer glucose between phenolic acids, phytohormones, and
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