Endo-β-mannanase and β-mannosidase activities in rice grains during and following germination, and the influence of gibberellin and abscisic acid

2005 ◽  
Vol 15 (3) ◽  
pp. 219-227 ◽  
Author(s):  
Aoxue Wang ◽  
Xiaofeng Wang ◽  
Yanfang Ren ◽  
Xuemei Gong ◽  
J. Derek Bewley

Grains of indica rice (Oryza sativa cv. Peiza 67) exhibit an increase in endo-β-mannanase activity, mostly after the completion of germination. According to tissue blots, the initial increase occurs in association with the embryo, and possibly the scutellum, although the largest sustained increase in activity is in the peripheral regions of the endosperm. The aleurone layer, being the only living region of the endosperm, is presumably the site of synthesis and secretion of the enzyme into the non-living, starch-laden region. β-Mannosidase activity is low throughout germination and subsequent seedling growth, particularly in the endosperm regions. Its activity profile does not mimic that of endo-β-mannanase. In the intact grain, gibberellin (GA) causes a relatively small increase in endo-β-mannanase activity, while abscisic acid (ABA) causes a large decrease; this inhibition is overcome to a considerable extent when GA is supplied along with ABA. β-Mannosidase activity is little affected by either GA or ABA. Embryoless half-grains imbibed in water exhibit only a small increase in endo-β-mannanase activity with time of imbibition, showing the necessity for a stimulus from the embryo for this to occur. Incubating half-grains in the presence of GA results in a large increase in enzyme activity; ABA reduces the amount of activity compared to the water controls. GA is capable of reversing the inhibitory effect of ABA with respect to endo-β-mannanase activity. As in the intact grains, β-mannosidase activity in the half-grains is unaffected by either GA or ABA. It is concluded that the major site for the production of endo-β-mannanase activity is the aleurone layer, and this event is influenced by the presence of the embryo; in the absence of the latter, the increase in enzyme activity is stimulated by GA. β-Mannosidase activity is low throughout germination and post-germination, it is not influenced by GA and ABA, and thus its activity is not regulated in a coordinated manner with that of endo-β-mannanase.

1996 ◽  
Vol 6 (1) ◽  
pp. 23-29 ◽  
Author(s):  
Fanouris Kontos ◽  
Caroline G. Spyropoulos ◽  
Alison Griffen ◽  
J. Derek Bewley

AbstractEndosperms of fenugreek and carob which have been leached following their isolation exhibit increased activity of endo-β-mannanase, part of which is released into the surrounding incubation medium. This activity was suppressed by the addition to the endosperms of abscisic acid or endosperm/seed coat leachate. The leachate from carob inhibited the increase of endo-β-mannanase activity in fenugreek and that from fenugreek inhibited enzyme activity in carob but more weakly; neither of these leachates inhibited the production of α-amylase in wheat endosperm. Polyethylene glycol-induced stress on non-leached endosperms inhibited endo-β-mannanase production, but not when the stress was applied following endosperm leaching. However, the stress did reduce the amount of enzyme released into the surrounding incubation medium. Several isoenzymes of mannanase could be detected on isoelectric focusing activity gels in the endosperms of both fenugreek and carob, but their pis differed between the two species. When activity was suppressed by ABA or leachate, all pl forms declined equally.


1975 ◽  
Vol 53 (24) ◽  
pp. 3041-3050 ◽  
Author(s):  
C. H. A. Little

In experiments with attached and detached shoots of balsam fir, Abies balsamea L., synthetic (±)abscisic acid (ABA) (1) reduced photosynthesis and transpiration by inducing stomatal closure, (2) inhibited indoleacetic acid (IAA) - induced cambial activity in photosynthesizing and non-photosynthesizing shoots, and (3) inhibited the basipetal movement of [14C]IAA. Neither gibberellic acid nor kinetin counteracted the inhibitory effect of (±)ABA on IAA-induced cambial activity. In addition it was demonstrated that increasing the internal water stress increased the level of endogenous ABA in the phloem–cambial region of bark peelings and decreased the basipetal movement of [14C]IAA through branch sections. On the basis of these findings it is proposed that internal water stress inhibits cambial activity, partly through increasing the level of ABA; the ABA acts to decrease the provision of carbohydrates and auxin that are required for cambial growth.


1974 ◽  
Vol 82 (1) ◽  
pp. 113-116 ◽  
Author(s):  
M. Abdel-Rahman ◽  
F. M. R. Isenberg

SUMMARYExperiments were conducted to study the effect of plant injection with growth regulators on the dormancy of onion bulbs cv. Elba Globe. Application of abscisic acid induced early senescence of the leaves and prolonged the rest period of the bulbs. This effect was partially overcome by subsequent applications of gibberellin, auxin or cytokinin and totally overcome with the application of a mixture of the three hormones. Maleic hydrazide application prolonged the rest period by inhibiting both sprouting and rooting of the bulbs throughout the storage period. This inhibitory effect was not overcome by the subsequent application of auxin, gibberellin, kinetin, or their combinations. Ethephon application increased rooting of bulbs and partially overcame the effect of abscisic acid on dormancy.


1979 ◽  
Vol 34 (9-10) ◽  
pp. 715-720 ◽  
Author(s):  
Gerhild Nurmann ◽  
Dieter Strack

Abstract From cotyledons of Raphanus sativus (red radish) an esterase activity which catalyzes the hy­drolysis of sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optimum of 8.5 and the apparent Km is 1.95 × 10-5 m. The enzyme is relatively insensi­tive to both physostigmine (eserine) {Ki = 1.73 × 10-4 m) and neostigmine (Ki = 2 .1 3 × 10-4 ᴍ). Diisopropyl fluorophosphate (DFP) showed no inhibition and diethyl p-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10-5 ᴍ, respectively. Choline (10-2 ᴍ) was inhibitory but acetylcholine (10-2 ᴍ) stimulated the enzyme activity.


2020 ◽  
Vol 42 ◽  
Author(s):  
Marcone Moreira Santos ◽  
Eduardo Euclydes de Lima e Borges ◽  
Glauciana da Mata Ataíde ◽  
Raquel Maria de Oliveira Pires ◽  
Debora Kelli Rocha

Abstract: Recent studies indicate that global temperatures will rise substantially in the 21st century, leading to the extinction of several plant species, as plant metabolism and germination are greatly affected by temperature. Melanoxylon brauna, a tree species native to the Atlantic Forest that occurs from northeastern to southeastern Brazil, is one of the many species threatened by global warming. Despite the economic and ecological importance of M. brauna, studies investigating the influence of heat stress on seed germination and biochemical responses are still incipient. This study aimed to evaluate enzyme activity in the micropylar region of M. brauna seeds during germination under heat stress conditions. Endo-β-mannanase, α-galactosidase, polygalacturonase, pectin methylesterase, pectin lyase, total cellulase, 1,3-β-glucosidase, and 1,4-β-glucosidase activities were determined in micropyles of seeds imbibed for 24, 48 and 72 h at 25, 35 and 45 °C. Seed germination was highest at 25 °C. Endo-β-mannanase activity was not detected under any of the experimental conditions, but imbibition temperature had a significant effect on the activity of all other enzymes.


Microbiology ◽  
2006 ◽  
Vol 152 (7) ◽  
pp. 2013-2021 ◽  
Author(s):  
Dongyi Xu ◽  
Xianwei Liu ◽  
Cong Guo ◽  
Jindong Zhao

Aldo-keto reductases (AKRs) are a superfamily of enzymes that reduce aldehydes and ketones, and have a broad range of substrates. An AKR gene, sakR1, was identified in the cyanobacterium Synechococcus sp. PCC 7002. A mutant strain with sakR1 inactivated was sensitive to glycerol, a carbon source that can support heterotrophic growth of Synechococcus sp. PCC 7002. It was found that the sakR1 null mutant accumulated more toxic methylglyoxal than the wild-type when glycerol was added to growth medium, suggesting that SakR1 is involved in the detoxification of methylglyoxal, a highly toxic metabolite that can damage cellular macromolecules. Enzymic analysis of recombinant SakR1 protein showed that it can efficiently reduce methylglyoxal with NADPH. Based on immunoblotting, SakR1 was not upregulated at an increased cellular methylglyoxal concentration. A pH-dependent enzyme-activity profile suggested that SakR1 activity could be regulated by cellular pH in Synechococcus sp. PCC 7002. The broad substrate specificity of SakR1 implies that SakR1 could play other roles in cellular metabolism.


Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4294 ◽  
Author(s):  
Salhab ◽  
Naughton ◽  
Barker

The inhibitory effect of new chemical entities on rat liver P450 marker activities was investigated in a functional approach towards drug development. Treatment of colorectal cancer (CRC) and chemoprevention using salicylic acid has gained a lot of attention, mainly in the prevention of the onset of colon cancer. Thus, an in vitro inhibitory effect of salicylic acid on rat CYP2C11 activity was examined by using high performance liquid chromatography (HPLC). High performance liquid chromatography analysis of a CYP2C11 assay was developed on a reversed phase C18 column (SUPELCO 25 cm × 4.6 mm × 5 µm) at 243 nm using 32% phosphate buffer (pH 3.36) and 68% methanol as a mobile phase. The CYP2C11 assay showed good linearity for all components (R2 > 0.999). Substrates and metabolites were found to be stable for up to 72 hours. Additionally, the method demonstrated good reproducibility, intra- and inter-day precision (<15%), acceptable recovery and accuracy (80%–120%), and low detection (1.3501 µM and 3.2757 µM) and quantitation limit values (4.914 µM and 9.927 µM) for 16α-hydroxytestosterone and testosterone, respectively. Salicylic acid acts reversibly as a noncompetitive (weak) inhibitor with Ki = 84.582 ± 2.67 µM (concentration of inhibitor to cause 50% inhibition of original enzyme activity (IC50) = 82.70 ± 2.67 µM) for CYP2C11 enzyme activity. This indicates a low potential to cause toxicity and drug–drug interactions.


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