Cyclodextrins as activator and inhibitor of latent banana pulp polyphenol oxidase

The effect of cyclodextrins (CDs) on o-diphenol oxidation catalyzed by banana polyphenol oxidase (PPO) was studied. The oxidation of dopamine, the natural substrate of banana, in the presence of cyclodextrins was unaffected, because this hydrophilic phenol does not form inclusion complexes with CDs. However, when a hydrophobic phenol such as tert-butylcatechol (TBC) was used, a marked inhibition was observed with beta-, hydroxypropyl-beta-, and maltosyl-beta- CDs. This inhibition was due to the complexation of TBC in the CD core, demonstrating that banana pulp PPO worked only toward free substrate and not toward the complex TBC-CDs. In addition, the effect of some inhibitors in the presence of CDs and dopamine as substrate was studied. Increasing concentrations of CDs, in the presence of two inhibitors (4-iodophenol and cinnamic acid) were able to activate the inhibited enzyme to reach the noninhibited level by complexing the inhibitors in the hydrophobic core of the CDs. This dual effect of CDs as activator and inhibitor was tested in crude banana pulp extracts, with surprising activation effects never before described being observed.     

Kinetics of activation of latent mushroom (Agaricus bisporus) tyrosinase by benzyl alcohol.

A latent isoform of Agaricus bisporus tyrosinase has been isolated and activated by benzyl alcohol, one of the major volatile compounds in mushrooms of this genus. The progress curve that describes the activation process reached the steady-state rate (V(ss)) after a lag period (tau). The rate of active tyrosinase formation was calculated by coupling the oxidation of o-diphenols to the activation process. V(ss) depended on benzyl alcohol, o-diphenol, and latent tyrosinase concentrations. The lag period depended on benzyl alcohol concentrations but not on o-diphenol and enzyme concentrations. The size of the latent mushroom tyrosinase was 67 kDa, determined by SDS-PAGE and Western blotting assays. This size was not modified after activation by benzyl alcohol. The presence of a lag period and the lack of change of the molecular mass of the protein after activation could indicate a slow conformational change of the protein to render the final active form. The values of the kinetic constants V(max) and K(m) on the o-diphenols 4-tert-butylcatechol, L-DOPA, and dopamine were different between the latent tyrosinase activated by benzyl alcohol and the commercial tyrosinase. They might indicate that a different final active tyrosinase, depending on the activator used, could arise.     

Purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) pulp

Polyphenol oxidase (EC 1.10.3.1, PPO) in the pulp of banana (Musa sapientum L.) was purified to 636-fold with a recovery of 3.0%, using dopamine as substrate. The purified enzyme exhibited a clear single band on polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate (SDS)-PAGE. The molecular weight of the enzyme was estimated to be about 41000 and 42000 by gel filtration and SDS-PAGE, respectively. The enzyme quickly oxidized dopamine, and its K(m) value for dopamine was 2.8 mM. The optimum pH was at 6.5, and the enzyme activity was stable in the range of pH 5-11 at 5 degrees C for 48 h. The enzyme had an optimum temperature of 30 degrees C and was stable even after a heat treatment at 70 degrees C for 30 min. The enzyme activity was completely inhibited by L-ascorbic acid, cysteine, sodium diethyldithiocarbamate, and potassium cyanide. Under a low buffer capacity, the enzyme was also strongly inhibited by citric acid and acetic acid at 10 mM.     

Effect of calcium on the oxidation of linoleic acid by potato (Solanum tuberosum var. Desiree) tuber 5-lipoxygenase

When the effect of calcium on the oxidation of linoleic acid by potato tuber 5-lipoxygenase (LOX) was investigated, it was seen to promote the enzyme's activity at pH values higher than the optimum pH of 6.3, resulting in an enzyme activation at alkaline pH. Kinetic analysis of calcium activation at different pH values revealed that the cation abolished the inhibition by high substrate concentration, which occurs in the absence of Ca(2+), thus leading to activation at high substrate concentration. Studies were conducted to investigate the influence of Ca(2+) on the physicochemical nature of the substrate and its effect on the LOX activity expression. It was concluded that the aggregation mode rather than the aggregation state of linoleic acid is responsible for potato 5-LOX changes.     

Pseudoperoxidase activity of myoglobin: kinetics and mechanism of the peroxidase cycle of myoglobin with H2O2 and 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) as substrates

Using 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) as substrate, it has been shown that the increased peroxidase activity for decreasing pH of myoglobin activated by hydrogen peroxide is due to a protonization of ferrylmyoglobin, MbFe(IV)=O, facilitating electron transfer from the substrate and corresponding to pK(a) approximately 5.2 at 25.0 degrees C and ionic strength 0.16, rather than due to specific acid catalysis. On the basis of stopped flow absorption spectroscopy with detection of the radical cation ABTS(.+), the second-order rate constant and activation parameters for the reaction between MbFe(IV)=O and ABTS were found to have the values k = 698 +/- 32 M(-1) s(-1), DeltaH# = 66 +/- 4 kJ mol(-1), and DeltaS# = 30 +/- 15 J mol(-1) K(-1) at 25.0 degrees C and physiological pH (7.4) and ionic strength (= 0.16 M NaCl). At a lower pH (5.8) corresponding to the conditions in meat, values were found as follows: k = 3.5 +/- 0.3 x 10(4) M(-1) s(-1), DeltaH# = 31 +/- 6 kJ mol(-1), and DeltaS# = -53 +/- 19 J mol(-1) K(-1), indicative of a shift from outersphere electron transfer to an innersphere mechanism. For steady state assay conditions, this shift is paralleled by a shift from saturation kinetics at pH 7.4 to first-order kinetics for H2O2 as substrate at pH 5.8. In contrast, the activation reaction between myoglobin and hydrogen peroxide was found at 25.0 degrees C to be slow and independent of pH with values of 171 +/- 7 and 196 +/- 19 M(-1) s(-1) found at physiological and meat pH, respectively, as determined by sequential stopped flow spectroscopy, from which a lower limit of k = 6 x 10(5) M(-1) s(-1) for the reaction between perferrylmyoglobin, .MbFe(IV)=O, and ABTS could be estimated. As compared to the traditional peroxidase assay, a better characterization of pseudoperoxidase activity of heme pigments and their denatured or proteolyzed forms is thus becoming possible, and specific kinetic effects on activation, substrate oxidation, or shift in rate determining steps may be detected.     

Analysis and modeling of the ferulic acid oxidation by a glucose oxidase-peroxidase association. Comparison with a hexose oxidase-peroxidase association

A commercial glucose oxidase (GOX) from Aspergillus niger was partially characterized. The enzyme exhibited a two-step transfer mechanism, and the kinetic constants toward glucose and oxygen were determined. Under conditions similar to dough making (glucose concentration and pH), GOX does not exhibit maximum activity. A hexose oxidase (HOX) from Chondrus crispus was partially characterized as well. The HOX activity is not far from the optimum in the kneading conditions (pH and glucose concentration). A peroxidase (POD) purified from wheat germ was used to oxidize ferulic acid in the presence of GOX or HOX. Hydrogen peroxide produced during the glucose oxidation activates the wheat germ POD. Ferulic acid oxidation in solutions containing different ratios of POD + GOX or HOX + POD was followed by UV spectrophotometry. For the same dosage, the HOX-POD system is the most efficient for peroxidase activation. Using absorbance data and kinetic constants of GOX and POD, a mathematical model describing the release or consumption of the different reactants (hydrogen peroxide, oxygen, and ferulic acid) in the medium was developed, and experimental data correlated well with calculated values. The results obtained will be applied to investigate the effect of GOX and HOX activities on the rheological properties of dough.     

Kinetic study of the activation of banana juice enzymatic browning by the addition of maltosyl-beta-cyclodextrin

In recent years, the use of cyclodextrins (CDs) as antibrowning agents in fruit juices has received growning attention. However, there has been no detailed study of the behavior of these molecules as substances, which can lead to the darkening of foods. In this paper, when the color of fresh banana juice was evaluated in the presence of different CDs, the evolution of several color parameters was the opposite of that observed in other fruit juices. Moreover, a kinetic model based on the complexation by CDs of the natural browning inhibitors present in banana is developed for the first time to clarify the enzymatic browning activation of banana juice. Finally, the apparent complexation constant between the natural polyphenoloxidase inhibitors present in banana juice and maltosyl-beta-CD was calculated (Kci = 27.026 +/- 0.212 mM (-1)).     

Oxidation of the flavonol quercetin by polyphenol oxidase

Because direct oxidation of flavonols by polyphenol oxidase (PPO) has not previously been reported and, given the importance of flavonols, the ability of broad bean seed PPO to oxidize the flavonol quercetin was studied. The reaction was followed by recording spectral changes with time. Maximal spectral changes were observed at 291 nm (increase) and at 372 nm (decrease). The presence of two isosbectic points (at 272 and 342 nm) suggested the formation of only one absorbent product. These spectral changes were not observed in the absence of PPO. The oxidation rate, which varied with pH, was highest at pH 5.0. The following kinetic parameters were also determined: V(m) = 11 microM/min, K(m) = 646 microM, V(m)/K(m) = 17 x 10(-)(2) min(-)(1). Flavonol oxidation was efficiently inhibited (K(I) = 3.5 microM) by specific PPO inhibitors such as 4-hexylresorcinol. The results obtained showed that quercetin oxidation was strictly dependent on the presence of PPO.     

Proteolytic activation of latent Paraguaya peach PPO. Characterization of monophenolase activity

The kinetics of the activation process of latent peach PPO by trypsin was studied. By coupling this activation process to the oxidation of 4-tert-butylcatechol (TBC) to its corresponding quinone, it was possible to evaluate the specific rate constant of active PPO formation, k(3), which showed a value of 0.04 s(-1). This proteolytic activation of latent peach PPO permitted us to characterize the monophenolase activity of peach PPO for the first time using p-cresol as substrate, and it showed the characteristic lag period of the kinetic mechanism of monophenols hydroxylation, which depended on the enzyme and substrate concentration, the pH and the presence of catalytic amounts of o-diphenol (4-methylcatechol). The enzyme activation constant, k(act), was 2 microM.     

Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase

In the present paper the catecholase and cresolase activities of eggplant polyphenol oxidase (PPO) are described. To preserve the latter activity, a partially purified enzyme was used. Peroxidase was removed from the preparation to avoid its interference with PPO during phenol oxidation. The partially purified eggplant PPO was fully active. The catecholase/cresolase ratio of 41.1 indicated that, in a pH close to the physiological, diphenol oxidation predominates over monophenol oxidation. The characteristic lag phase of the cresolase activity is modulated by the pH, the monophenol and diphenol concentrations, and the enzyme's concentration. The effect of several inhibitors was also tested, and the K(i) values of the two most effective (tropolone and 4-hexylresorcinol) were determined.     

Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel

Polyphenol oxidase (EC 1.10.3.1, o-diphenol: oxygen oxidoreductase, PPO) of banana (Musa sapientum L.) peel was partially purified about 460-fold with a recovery of 2.2% using dopamine as substrate. The enzyme showed a single peak on Toyopearl HW55-S chromatography. However, two bands were detected by staining with Coomassie brilliant blue on PAGE: one was very clear, and the other was faint. Molecular weight for purified PPO was estimated to be about 41 000 by gel filtration. The enzyme quickly oxidized dopamine, and its Km value (Michaelis constant) for dopamine was 3.9 mM. Optimum pH was 6.5 and the PPO activity was quite stable in the range of pH 5-11 for 48 h. The enzyme had an optimum temperature at 30 degrees C and was stable up to 60 degrees C after heat treatment for 30 min. The enzyme activity was strongly inhibited by sodium diethyldithiocarbamate, potassium cyanide, L-ascorbic acid, and cysteine at 1 mM. Under a low buffer capacity, the enzyme was also strongly inhibited by citric acid and acetic acid at 10 mM.     

Kinetic studies of lycopene isomerization in a tributyrin model system at gastric pH

A semi-preparative HPLC method was developed in order to isolate and purify the 13-cis-lycopene isomer in tomato-based materials. The result was compared with the naturally predominant all-trans-lycopene isomer, in terms of stability to gastric pH at physiological temperature in a tributyrin model system. Kinetic experiments confirmed that lycopene isomerization is a reversible reaction, and under these conditions the all-trans isomer is more stable than the 13-cis isomer. In addition, it was found that at gastric pH 13-cis-lycopene would predominantly isomerize to the all-trans form rather than undergo oxidation/breakdown. A simulation based on the rate constants calculated in the kinetic study indicated that at gastric pH the lycopene isomeric distribution aimed toward an equilibrium characterized by approx 16% 13-cis-, 16% 9-cis-, and 68% all-trans-lycopene. This study suggests that pH-driven isomerization in the stomach is at least partially responsible for the relatively high cis-lycopene proportion found in vivo.     

碱性肥料对香蕉枯萎病发生及土壤微生物群落的影响

【目的】针对我国香蕉主产区蕉园土壤酸化、 微生物环境恶化,香蕉枯萎病严重泛滥和肆虐,严重威胁产业等问题,通过施用碱性肥料改善蕉园土壤酸性及微生物环境,从而降低香蕉枯萎病发病率,促进香蕉健康生长。【方法】以重病区蕉园土壤为对象,采用盆栽试验,研究碱性肥料对土壤微生物及香蕉枯萎病发生情况的影响。试验设碱性肥料(AF)和常规肥料(CCF)2种肥料处理,每种肥料设低量(L1)、 中量(L2)和高量(L3)3个施肥量,同一施肥量处理的氮、 磷、 钾总用量相等。于2013年3月6日移栽香蕉苗到营养钵, 130 d后待各处理香蕉发病明显时采集土壤及植株样品进行各项指标测定。【结果】 1)施碱性肥料能显著降低香蕉枯萎病的发病率,常规肥料处理的香蕉发病率为78%,而碱性肥料处理的仅为33%。2)碱性肥料对土壤微生物群落有明显的影响,土壤中的真菌数量AF处理明显少于CCF处理,而细菌、 放线菌数量则显著高于CCF处理,因此AF处理土壤的香蕉尖孢镰刀菌明显减少。3)试验期间碱性肥料能显著提高土壤pH值,较常规肥料处理提高了0.75个pH单位,而土壤EC值比常规肥料处理低47.76 μS/cm。4)土壤pH值与土壤中古巴专化型尖孢镰刀菌(FOC)的数量及香蕉发病率呈显著负相关; 细菌数量与FOC数量、 香蕉枯萎病发病率、 病情指数之间呈显著的负相关; 土壤中FOC和真菌数量与香蕉发病率呈显著正相关。5)香蕉生物量随着碱性肥料和常规肥料用量的增大而增加,但碱性肥料的效果更加明显。【结论】应用碱性肥料不仅可以为香蕉提供氮、 磷、 钾养分,而且能改良蕉园土壤酸性从而改善土壤微生物群落结构及环境,有效防控香蕉枯萎病的发生。     

采用改进YOLOv5的蕉穗识别及其底部果轴定位

为提高香蕉采摘机器人的作业效率和质量,实现机器人末端承接机构的精确定位,该研究提出一种基于YOLOv5算法的蕉穗识别,并对蕉穗底部果轴进行定位的方法。将CA（Coordinate Attention）注意力机制融合到主干网络中,同时将C3（Concentrated-Comprehensive Convolution Block）特征提取模块与CA注意力机制模块融合构成C3CA模块,以此增强蕉穗特征信息的提取。用 EIoU（Efficient Intersection over Union）损失对原损失函数CIoU（Complete Intersection over Union）进行替换,加快模型收敛并降低损失值。通过改进预测目标框回归公式获取试验所需定位点,并对该点的相机坐标系进行转换求解出三维坐标。采用D435i深度相机对蕉穗底部果轴进行定位试验。识别试验表明,与YOLOv5、Faster R-CNN等模型相比,改进YOLOv5模型的平均精度值（mean Average Precision, mAP）分别提升了0.17和21.26个百分点;定位试验表明,采用改进YOLOv5模型对蕉穗底部果轴定位误差均值和误差比均值分别为0.063 m和2.992%,与YOLOv5和Faster R-CNN模型相比,定位误差均值和误差比均值分别降低了0.022 m和1.173%,0.105 m和5.054%。试验实时可视化结果表明,改进模型能对果园环境下蕉穗进行快速识别和定位,保证作业质量,为后续水果采摘机器人的研究奠定了基础。     

Influence of potassium nutrition and the nitrate/ammonium ratio on the putrescine and spermidine contents in banana vitroplants

Potassium (K) is required in high doses by the banana (Musa sp.) plant and interacts with other nutrient elements in which banana tissues are maintained under in vitro condition as a consequence modifications in the plant metabolism take place mainly in nitrogen (N) compounds, such as proteins, amino acids, and secondary compounds. When K is present in concentrations lower than that required, diamines such as putrescine and poliamines are formed. This metabolic disorder can also be correlated with the presence of different inorganic N forms, such as nitrate (NO₃) and ammonium (NH₄), and the ratios between both ions as well. In order to follow the physiological performance of the interrelationships, K/putrescine and of the NO₃/NH₄ ratio in the tissue of banana vitroplantlets, shoot apex of two banana cvs. Nanica and Prata Ana were maintained in modified MS medium in the presence of six different doses of K: 5, 10, 15, 20, 25, and 30 mM. After the period of tissue proliferation the cultures were transferred to rooting media containing the same different K doses. Dry matter, K, putrescine, and spermidine contents and their accumulation were determined in the shoots and roots of the vitroplantlets and in the shoot apex of the expiant donor cultivar as well as the corresponding values for the whole vitroplantlets calculated. The data were statistically analyzed. The contents and accumulations of putrescine and spermidine in banana tissues were enhanced as K concentration decreased in the medium: four times (0.19% of the dry matter) for cv. Nanica and eight times (0.25% of the dry matter) for cv. Prata Ana. This behavior was not only related to the K depletion but to the NO₃/NH₄ ratio as well.     

Diphenol activation of the monophenolase and diphenolase activities of field bean (Dolichos lablab) polyphenol oxidase

This paper reports a study on the hydroxylation of ferulic acid and tyrosine by field bean (Dolichos lablab) polyphenol oxidase, a reaction that does not take place without the addition of catechol. A lag period similar to the characteristic lag of tyrosinase activity was observed, the length of which decreased with increasing catechol concentration and increased with increasing ferulic acid concentration. The activation constant K(a) of catechol for ferulic acid hydroxylation reaction was 5 mM. The kinetic parameters of field bean polyphenol oxidase toward ferulic acid and tyrosine were evaluated in the presence of catechol. 4-Methyl catechol, L-dihydroxyphenylalanine, pyrogallol, and 2,3,4-trihydroxybenzoic acid, substrates with high binding affinity to field bean polyphenol oxidase, could stimulate this hydroxylation reaction. In contrast, diphenols such as protocatechuic acid, gallic acid, chlorogenic acid, and caffeic acid, which were not substrates for the oxidation reaction, were unable to bring about this activation. It is most likely that only o-diphenols that are substrates for the diphenolase serve as cosubstrates by donating electrons at the active site for the monophenolase activity. The reaction mechanism for this activation is consistent with that proposed for tyrosinase (Sanchez-Ferrer, A.; Rodriguez-Lopez, J. N.; Garcia-Canovas, F.; Garcia-Carmona, F. Biochim. Biophys. Acta 1995, 1247, 1-11). The presence of o-diphenols, viz. catechol, L-dihydroxyphenylalanine, and 4-methyl catechol, is also necessary for the oxidation of the diphenols, caffeic acid, and catechin to their quinones by the field bean polyphenol oxidase. This oxidation reaction occurs immediately with no lag period and does not occur without the addition of diphenol. The kinetic parameters for caffeic acid (K(m) = 0.08 mM, V(max) = 32440 u/mg) in the presence of catechol and the activation constant K(a) of catechol (4.6 mM) for this reaction were enumerated. The absence of a lag period for this reaction indicates that the diphenol mechanism of diphenolase activation differs from the way in which the same o-diphenols activate the monophenolase activity.     

碱性长效缓释氮肥对蕉园土壤pH和香蕉氮肥利用效率的影响

【目的】近年来由于超量施用化肥导致蕉园土壤严重酸化,土壤生产力逐年明显下降,香蕉产量骤降,传统产区栽培面积锐减。为此本试验在超高密度栽培条件下,以碱性长效缓释氮肥（ALNF,N 22%）作为供试肥料,研究其降低土壤酸度的效果及对香蕉产量和氮肥利用率的影响,并进一步探讨肥料的碱性能否造成氮素的损失。 【方法】本研究包括两个试验,分别为肥料种类和肥料用量对比试验,香蕉栽培密度均为3333 plant/hm2。试验1为碱性长效缓释肥料（ALNF）、控释配方BB肥料（CRF_BB）、常规肥料（CCF）三因素对比试验,以无氮处理（CK）为对照。试验2为完全ALNF（N 337.5 g/plant）,ALNF+60 g尿素N（ACF1,397.5 g/plant）,ALNF+90 g尿素N（ACF2,427.5 g/plant）,以不施氮肥（CK）为对照。 【结果】超高密度栽培条件下,ALNF处理收获期土壤pH值分别比CRF_BB、CCF、CK、ACF1和ACF2处理提高了1.2、1.2、1.1、0.6和0.3个单位。ALNF和CRF_BB处理香蕉单株产量分别比CCF处理增加了43.4%和35.1%,ALNF和ACF1处理香蕉单株产量分别比ACF2增加了50.6%和40.0%。就氮素平衡而言,CRF_BB和ALNF处理作物携出氮量分别比CCF处理提高了48.9%和24.8%;CCF的氮素表观损失量最多,是ALNF处理的2.3倍;ALNF处理的土壤氮素残留量最多,分别是CRF_BB、CCF处理的1.6倍、2.4倍;ALNF处理香蕉的携氮量分别比ACF1、ACF2处理提高了5.0%、31.9%,土壤残留氮量增加了60.8%、162.6%,ALNF的氮素表观损失最少,并随着尿素添加量的增加而增加,ALNF处理的氮素表观损失量仅为ACF2的1/4。CRF_BB和ALNF处理的氮肥利用率分别比CCF的提高了66.7%、33.7%,ALNF处理比ACF1、ACF2处理提高了27.8%、87.7%,ACF1处理的比ACF2处理提高了46.9%。 【结论】碱性长效缓释氮肥能够显著降低土壤酸度,土壤pH提高了0.3~1.2个单位,提高香蕉产量35%~50%,增加香蕉氮素吸收量24%~50%,增加土壤氮素残留量,减少氮素表观损失,提高氮肥利用率27%~67%。单独施用碱性长效缓释氮肥不会造成氮素损失,但是碱性长效缓释氮肥与尿素混合使用会造成氮素损失并降低氮肥利用率。     

杨梅澄清汁及浓缩汁中花色苷热降解动力学的研究

杨梅花色苷易受温度、pH值等因素的影响而发生降解，是导致产品外观品质变劣的主要原因。本文研究了杨梅澄清汁及浓缩汁内花色苷在不同pH值和不同加热温度下的热稳定性。花色苷降解动力学数据的分析结果表明：杨梅花色苷热降解属动力学一级反应，随着pH值和温度的升高，杨梅花色苷降解的半衰期(t_1/2)和热降解活化能(Ea)显著下降，即花色苷的降解速度增大；同一处理条件下，浓缩果汁的t_1/2明显低于澄清汁。而反应速率常数k和Ea值大于澄清果汁，说明澄清汁花色苷的热稳定性优于浓缩汁。     

Does oxidation affect the water functionality of myofibrillar proteins?

Water-binding properties of myofibrils extracted from porcine muscle, and added hemoglobin with and without exposure to H2O2, were characterized using low-field proton NMR T2 relaxometry. The effects of pH and ionic strength in the samples were investigated as pH was adjusted to 5.4, 6.2, and 7.0 and ionic strength was adjusted to 0.29, 0.46, and 0.71 M, respectively. The formation of dityrosine as a measure of oxidative protein cross-linking revealed a significant increase in dityrosine concentrations upon H2O2 activation. The formation of dityrosine was strongly pH-dependent and increased with decreasing pH. In addition, increased levels of thiobarbituric acid reactive substances were observed upon addition of H2O2, implying that lipid oxidation was enhanced, however, with a different oxidation pattern as compared to the myofibrillar proteins. Low-field NMR relaxation measurements revealed reduced T2 relaxation times upon H2O2 activation, which corresponds to reduced water-holding capacity upon oxidation. However, a direct relationship between degree of oxidation and T2 relaxation time was not observed with various pH values and ionic strengths, and further studies are needed for a complete understanding of the effect of oxidation on myofibrillar functionality.     

Two types of oxidative dimerization of the black tea polyphenol theaflavin.

Theaflavin and its galloyl esters are polyphenolic pigments of black tea. In the course of studies on the oxidation mechanism of tea polyphenols, two theaflavin oxidation products named bistheaflavins A and B were isolated, and their structures were elucidated on the basis of MS and NMR spectroscopic analyses. Treatment of a mixture of (-)-epicatechin and (-)-epigallocatechin with banana fruit homogenate yielded bistheaflavin A together with theaflavin and theanaphthoquinone. The symmetrical structure of bistheaflavin A suggested that this compound was formed by oxidative C [bond] C coupling of two theaflavin molecules. In contrast, theaflavin in phosphate buffer (pH 7.3) was gradually oxidized to give bistheaflavin B and theanaphthoquinone. Bistheaflavin B possesses a bicyclooctane skeleton probably formed by intermolecular cyclization between dehydrotheaflavin and dihydrotheanaphthoquinone.