Rate Of Denaturation Research Articles

Physicochemical changes in cooked prawn muscle with or without shell during water bath treatment: Effect of thermal protein denaturation

AbstractThe presence or absence of prawn shell impacts the cooked muscle quality. Here, we evaluated the effect of different cooking temperatures and times during water bath treatment on the quality attributes of peeled and unpeeled prawns. Several factors, including heat penetration, moisture content, color distribution, microstructure, and texture changes were tested. Thermal protein denaturation was assessed to clarify differences in quality attributes between both samples. Heat penetration was slightly slower in unpeeled prawns compared to peeled prawns, which correlated with the lower denaturation rate for each protein (myosin, sarcoplasmic‐collagen, and actin). The tissue connection between the shell and muscle protects the prawn meat from shrinkage, resulting in reduced water release. Maximum stress at 50, 65, and 75°C was significantly higher in unpeeled prawns than in peeled prawns. However, the absence of shell resulted in a denser microstructure and slightly higher color profile in peeled prawns. These findings may be applied for the thermal processing of prawns.Practical ApplicationsThe applications of the findings of this study include but are not limited to: (a) predicting the thermal protein denaturation conditions for both peeled and unpeeled prawn muscles, which can facilitate the selection of the applied thermal process degree in order to reduce cooking losses, (b) direct mapping of color distribution at the surface and internal sections of both samples, which contribute to the acceptability of cooked prawn products and easy detection of overcooked areas, and (c) helping in the sensitization of consumers and also processors of the quality attribute retention of processed prawns, since prawns are processed with or without peeling as desired by the target customer

Effect of heating milk on whey protein denaturation and cheese-making properties

The cheese-making properties of milk heated at 80 °C for different times (0–8 min), and mixtures of severely-heated milk (80 °C, 30 min) with non-heated milk were evaluated in separate experiments. In both approaches, milk pH was adjusted to 6.3, 6.7 or 7.0 before heating. Despite different distributions of denatured whey protein (WP) between casein micelle surface and serum phase, heating pH had no significant effect on cheese-making properties. The two approaches were compared by reporting the results as a function of WP denaturation rate in milk. The mixed milk approach showed a higher detrimental effect on rennet-induced coagulation kinetics and curd contraction capacity during cooking than the heated milk approach. For similar WP-denaturation rate, higher yield was obtained for the mixed milk than the heated milk as a result of the better protein retention and larger increase of cheese moisture.

Femtosecond Laser Pulse Excitation of DNA-Labeled Gold Nanoparticles: Establishing a Quantitative Local Nanothermometer for Biological Applications.

Femtosecond (fs) laser pulsed excitation of plasmonic nanoparticle (NP)-biomolecule conjugates is a promising method to locally heat biological materials. Studies have demonstrated that fs pulses of light can modulate the activity of DNA or proteins when attached to plasmonic NPs; however, the precision over subsequent biological function remains largely undetermined. Specifically, the temperature the localized biomolecules "experience" remains unknown. We used 55 nm gold nanoparticles (AuNPs) displaying double-stranded (ds) DNA to examine how, for dsDNA with different melting temperatures, the laser pulse energy fluence and bulk solution temperature affect the rate of local DNA denaturation. A universal "template" single-stranded DNA was attached to the AuNP surface, and three dye-labeled probe strands, distinct in length and melting temperature, were hybridized to it creating three individual dsDNA-AuNP bioconjugates. The dye-labeled probe strands were used to quantify the rate and amount of DNA release after a given number of light pulses, which was then correlated to the dsDNA denaturation temperature, resulting in a quantitative nanothermometer. The localized DNA denaturation rate could be modulated by more than threefold over the biologically relevant range of 8-53 °C by varying pulse energy fluence, DNA melting temperature, and surrounding bath temperature. With a modified dissociation equation tailored for this system, a "sensed" temperature parameter was extracted and compared to simulated AuNP temperature profiles. Determining actual biological responses in such systems can allow researchers to design precision nanoscale photothermal heating sources.

Transmembrane Pressure and Recovery of Serum Proteins During Microfiltration of Skimmed Milk Subjected to Different Storage and Treatment Conditions.

Milk pre-processing steps-storage at 4 °C (with durations of 48, 72 or 96 h) and methods for microbiological stabilization of milk (1.4 μm microfiltration, thermization, thermization + bactofugation, pasteurization) are performed industrially before 0.1 µm-microfiltration (MF) of skimmed milk to ensure the microbiological quality of final fractions. The objective of this study was to better understand the influence of these pre-processing steps and their cumulative effects on MF performances (i.e., transmembrane pressure, and transmission and recovery of serum proteins (SP) in the permeate). Results showed that heat treatment of skimmed milk decreased ceramic MF performances, especially after a long 4 °C storage duration (96 h) of raw milk: when milk was heat treated by pasteurization after 96 h of storage at 4 °C, the transmembrane pressure increased by 25% over a MF run of 330 min with a permeation flux of 75 L·h−1·m−2 and a volume reduction ratio of 3.0. After 48 h of storage at 4 °C, all other operating conditions being similar, the transmembrane pressure increased by only 6%. When milk was 1.4 µm microfiltered, the transmembrane pressure also increased by only 6%, regardless of the duration of 4 °C storage. The choice of microbiological stabilization method also influenced SP transmission and recovery: the higher the initial heat treatment of milk, the lower the transmission of SP and the lower their recovery in permeate. Moreover, the decline of SP transmission was all the higher that 4 °C storage of raw milk was long. These results were explained by MF membrane fouling, which depends on the load of microorganisms in the skimmed milks to be microfiltered as well as the rate of SP denaturation and/or aggregation resulting from pre-processing steps.

Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins

The effect of the addition of caseinomacropeptide (CMP) or desialylated CMP on the heat-induced denaturation and aggregation of whey proteins was investigated in the pH range 3 to 7 after heating at 80°C for 30 min. The rate and temperature of denaturation, the extent of aggregation, and the changes in secondary structure of the whey proteins heated in presence of CMP or desialylated CMP were measured. The sialic acid bound to CMP favored the denaturation and aggregation of whey proteins when the whey proteins were oppositely charged to CMP at pH 4. A transition occurred at pH 6, below which the removal of sialic acid enhanced the stabilizing properties of CMP against the denaturation and aggregation of the whey proteins. At pH >6, the interactions between desialylated CMP and the whey proteins led to more extensive denaturation and aggregation. Sialic acid bound to CMP influenced the denaturation and aggregation behavior of whey proteins in a pH-dependent manner, and this should be considered in future studies on the heat stability of such systems containing CMP.

Kinetic modelling of the heat stability of bovine lactoferrin in raw whole milk

The thermal denaturation of the naturally occurring lactoferrin in raw bovine whole milk has been measured over a range of temperatures from 65 to 121 °C for holding times from 2 up to 300 s designed to mimic heating processes used in the food manufacturing industry. Data were generated by heat treatments of raw whole milk from two different sources, New Zealand (NZ) and China, and with lactoferrin at two different levels of naturally occurring iron saturation. Denaturation rates for lactoferrin in the Chinese-sourced milk samples were at least two-fold greater than lactoferrin in the NZ milk over the temperature range 65–80 °C. At 85 °C rates of denaturation were the same although more than 80-fold greater than at 65 °C whereas, at 95 °C, lactoferrin in the NZ milk denatured at twice the rate of that in the Chinese milk. The differences in denaturation rates up to 80 °C likely reflected the greater heat stability of the more iron-saturated NZ milk samples. From these data, a combined kinetic and Arrhenius-based model has been developed and validated that allows calculation of native lactoferrin retained after thermal processing at any temperature-time combination in the experimental range (65–95 °C). This model should have applicability in the evaluation of existing processes and for the design of processes to improve the retention of lactoferrin during food manufacture.

Kinetics of denaturation and aggregation of highly concentrated β-Lactoglobulin under defined thermomechanical treatment

The influence of thermomechanical treatment (temperature 60 °C – 100 °C and shear rate 0.05 s−1 – 50 s−1) on the denaturation and aggregation of β-Lactoglobulin at high concentrations (50 % – 70 %) was investigated. While denaturation and aggregation reaction rate decreased at higher concentrations, a combination of heat and mechanical treatment resulted in an increase in reaction rates and consequently, in higher degrees of non-disulfide covalent bond aggregation. The kinetic parameters were determined by non-linear regression. Denaturation (combined effect of unfolding and aggregation) and covalent bond aggregation were found to follow 2.15 and 1.7 order kinetics, respectively. At the investigated conditions, the activation energy calculated for the denaturation and covalent bond aggregation reaction ranged from 25 to 283 kJ mol−1. Although the activation energy for the denaturation and aggregation reactions decreases with increasing shear rate, it was found that the mechanical treatment mainly affected the reactions at high temperatures, probably due to the increased molecular motion.

Comparative study on emulsifying and physico-chemical properties of bovine and camel acid and sweet wheys

Main goal of this research was to examine the emulsifying properties of acid and sweet wheys extracted from bovine and camel fresh milks after heating at 70 and 90 °C for 30 min at laboratory scale. Specifically, emulsifying properties (emulsification stability (ESI) and activity (EAI) indexes) and the physico-chemical characteristics (surface hydrophobicity, ζ-potential, interfacial tension and denaturation rate) of wheys were assessed. Maximum EAI and ESI were found for sweet wheys (EAI~ 2 m2/g; ESI~ 65%), with higher EAI values for the camel whey. This behavior was explained by the strongest electrostatic-repulsive forces between oil droplets under conditions away from the isoelectric-point of proteins in agreement with the ζ-potential measurements.Findings indicate that heating affected the physico-chemical properties of camel and bovine whey proteins in acidic conditions by increasing surface hydrophobicity and the ability to reduce the interfacial tension. These results confirmed the protein-protein aggregation of heated acid wheys as proved by electrophoreses.

Effect of EGCG-gelatin biofilm on the quality and microbial composition of tilapia fillets during chilled storage

The effects of the (−)-Epigallocatechin gallate (EGCG)-gelatin biofilm treatment (EGT) on microbial composition and quality of tilapia fillets stored at low temperatures were evaluated. The changes in mechanical properties, microbial reproduction, as well as lipid and protein oxidation during fillets storage were determined. The results showed that EGT reduced the microbial count and the relative abundance of the fillets. And EGT delayed the rate of lipid oxidation and protein denaturation in fillets. Compared with the control group, EGT samples had lower K values (74% on 18 d) and biogenic amines (39 mg/kg for putrescine and 50 mg/kg for cadaverine on 21 d). According to sensory evaluation, the shelf life of tilapia fillets was extended by 6 d in the EGT group. Therefore, EGT improved the quality of cryopreserved tilapia fillets and could be considered as a potential method for fish fillet preservation.

The Effects of Storage on Quality and Nutritional Values of Ehrenberg's Snapper Muscles (Lutjanus Ehrenbergi): Evaluation of Natural Antioxidants Effect on the Denaturation of Proteins.

Protein denaturation in frozen minced fillets (Ehrenberg’s Snapper), stored at −25 °C was studied; 50.0 mg biomass/50g mince fillets treated with cinnamon, cumin, turmeric, garlic, ginger and 25.0 mg of vitamin C were used to slow protein denaturation. FT-IR stretching vibration of Amide-A (νNH) at 3300 cm−1; Amide-I stretching (νC=O) between 1600−1690 cm−1 and Amide-II stretching (νCN) and bending (δNH) between 1480 and 1575cm−1 were used as marker peaks. Garlic was the most significant (p ≤ 0.01) in controlling the rate of protein denaturation when νNH was used as a marker peak. DSC analysis showed that turmeric presented the highest effect on delaying the denaturation of sarcoplasmic proteins with a followed by garlic-treated mince fillets . All spices used were efficient in stopping the denaturation of myosin with the highest registered for cinnamon-treated mince fillets. Actin was less vulnerable to denaturation in comparison to myosin and sarcoplasmic proteins.

Optimum temperature may be a misleading parameter in enzyme characterization and application.

The optimum temperature is commonly determined in enzyme characterization. A search in the PubMed database for “optimum temperature” and “enzymes” yielded more than 1,700 manuscripts reporting this parameter over the last five years. Here, we show that the optimum temperature is not a constant. The catalytic activity of the mesophylic β-glucosidase Sfβgly was determined at different temperatures using different assay times and enzyme concentrations. We observed that the optimum temperature for Sfβgly changed by 5°C simply by modifying the assay length, and it was inversely correlated with enzyme concentration. These observations rely on the fact that close to the melting temperature, thermal denaturation continuously decreases the active enzyme concentration as the assay progresses. Thus, as the denaturation rate increases with increasing temperature, the bell-shaped curves observed in “activity versus temperature plots” occur only if the enzyme is denatured at and above the optimum temperature, which was confirmed using the thermostable β-glucosidase bglTm. Thus, the optimum temperature hardly reflects an intrinsic enzyme property and is actually a mere consequence of the assay condition. Thus, adoption of the “optimum temperature” determined under bench conditions for large-scale uses, which differ in assay length and enzyme concentration, may result in lower yields and financial losses.

Thermodynamics enhancement of Alternaria tenuissima KM651985 laccase by covalent coupling to polysaccharides and its applications

This study full filed in enhancement of catalytic, thermodynamics and storage stability of Alternaria tenuissima KM651985 laccase by conjugation to sodium periodate oxidized starch. The starch conjugated A. tenuissima KM651985 laccase was active over a wide range of temperatures and pHs with the highest activity at 60 °C and 4, respectively. The thermal stability of conjugated A. tenuissima KM651985 laccase was indicated by, high T1/2 values (half life) 1076.16, 382.42 and 191.23 min at 50, 60 and 70 °C, respectively, low Kd (denaturation rate constant) 6.44 × 10−4, 18.13 × 10−4 and 36.25 × 10−4 min−1 at the same temperatures, high D-values (decimal reduction time) 3575.56, 1270.61 and 635.38 min at the same temperatures. Also, the thermal stability of conjugated A. tenuissima KM651985 laccase was emphasized by high ΔHd (enthalpy), high ΔGd (free energy) and low ΔSd (entropy). The conjugated A. tenuissima KM651985 laccase showed high effectiveness in dyes decolorization of Remazol Brilliant Blue R (RBBR) and Malachite Green (MG). Moreover, the addition of conjugated A. tenuissima KM651985 laccase with hemicellulolytic enzymes cocktail improved the saccharification of corn cobs, rice straw, corn cobs leaves and water hyacinth with the highest reducing sugar production 847.44 ± 19.17 mg from corn cops.

UV-Denaturation Assay to Assess Protein Photostability and Ligand-Binding Interactions Using the High Photon Flux of Diamond B23 Beamline for SRCD.

Light irradiation with high photon flux in the vacuum and far-UV region is known to denature the conformation of biopolymers. Measures are in place at Diamond Light Source B23 beamline for Synchrotron Radiation Circular Dichroism (SRCD) to control and make this effect negligible. However, UV denaturation of proteins can also be exploited as a novel method for assessing biopolymer photostability as well as ligand-binding interactions. Usually, host–ligand binding interactions can be assessed monitoring CD changes of the host biopolymer upon ligand addition. The novel method of identifying ligand binding monitoring the change of relative rate of UV denaturation using SRCD is especially important when there are very little or insignificant secondary structure changes of the host protein upon ligand binding. The temperature study, another method used to determine molecular interactions, can often be inconclusive when the thermal effect associated with the displacement of the bound solvent molecules by the ligand is also small, making the determination of the binding interaction inconclusive. Herein we present a review on the UV-denaturation assay as a novel method to determine the relative photostability of protein formulations as well as the screening of ligand-binding interactions using the high photon flux Diamond B23 beamline for SRCD.

Effects of anionic and cationic surfactants on the rheological properties and kinetics of bovine serum albumin hydrogel

The effects of the anionic surfactant, sodium dodecyl sulfate (SDS), and of the cationic surfactant cetyltrimethylammonium bromide (CTAB) on the gelation kinetics of bovine serum albumin (BSA) hydrogel were investigated by rheological measurements using surfactant concentrations of 0–0.05 M, and BSA concentrations of 5, 7, and 10 wt%. It was found while an increase in CTAB concentration accelerated the rate of gelation of BSA solution under temperature jump and temperature ramp conditions, BSA solutions containing SDS exhibited a heat-dependent protective effect against thermal denaturation and gelation. Under temperature ramp conditions, inhibition of BSA gelation by SDS was diminished by increasing SDS concentration, while under temperature jump conditions, inhibition of BSA gelation increased with SDS concentration. That is, gel temperature (Tgel) under temperature ramp decreased with increasing CTAB and with SDS concentration, but under temperature jump the gel time (tgel) decreased with increasing CTAB concentration but increased with SDS concentration. Furthermore, BSA/CTAB solutions were found to gel more rapidly than BSA/SDS solutions, which was in line with the lower activation energy of BSA/CTAB gel. In support of experiments, molecular dynamics (MD) simulations and dynamic light scattering (DLS) revealed the faster rate of BSA denaturation in the presence of CTAB was responsible for the increased gelation rate of BSA/CTAB solutions, whereas BSA was found to be protected by SDS against thermal denaturation leading to the slower gelation rate of BSA/SDS solutions.

Improving the mesoscopic modeling of DNA denaturation dynamics

Although previously developed mesoscopic DNA models have successfully reproduced thermodynamic denaturation data, recent studies show that these overestimate the rate of denaturation by orders of magnitude. Using adapted Peyrard–Bishop–Dauxois (PBD) models, we have calculated the denaturation rates of several DNA hairpins and made comparison with experimental data. We show that the addition of a barrier at the onsite potential of the PBD model gives a more accurate description of the unzipping dynamics of short DNA sequences. The new models provide a refined theoretical insight on the dynamical mechanisms of unzipping which can have implications for the understanding of transcription and replication processes. Still, this class of adapted PBD models seems to have a fundamental limitation which implies that it is not possible to get agreement with available experimental results on the dynamics of long DNA sequences and at the same time maintain the good agreement regarding its thermodynamics. The reason for this is that the denaturation rate of long DNA chains is not dramatically lowered by the additional barrier—as the base-pairs that open are more likely to remain open, facilitating the opening of the full DNA molecule. Some care has to be taken, since experimental techniques suitable to the study of denaturation rates of long sequences seem not to agree with other experimental data on short DNA sequences. Further research, both theoretical and experimental, is therefore needed to resolve these inconsistencies—which will be a starting point for new minimalistic models that are able to describe both thermodynamics and dynamics at a predictive level.

Use of denatured whey protein in the production of artisanal cheeses from cow, goat and sheep milk

The objective of this study was to assess the potential of a whey protein (WP) heat-denaturation and recovery process adapted to small artisanal cheese plants. The effects of cheese’s milk origin (cow, goat or sheep) and cheese whey type (sweet or acid) on the recovery rates and characteristics of WP aggregates were evaluated. The influence of the WP aggregate addition and dispersion method on the cheese-making properties of milk was also investigated. Gravity separation combined with sediment drainage was compared to centrifugation for the recovery of WP aggregates, and showed similar or slightly lower recovery rates depending on milk origin. The higher WP denaturation rate in sheep whey (both sweet and acid) resulted in better protein-aggregate recovery when compared to goat or cow whey. The diameter of WP aggregates was affected by the dispersion method, and large aggregates (6.94–30.56 μm) were obtained with a rotor-stator disperser, and smaller aggregates (0.38–2.68 μm) were obtained with a valve homogenizer. Regardless of whey origin, adding larger-diameter WP aggregates to cheese milk had no negative impact on rennet-induced coagulation, whereas smaller aggregates decreased curd firmness. WP aggregates of both diameter ranges reduced curd contraction capacity, which increased the curd mass fraction and moisture after the cooking step. Adding WP aggregates to milk increased cheese yield and moisture, and the dispersion method had no influence on these parameters, suggesting that a valve homogenizer is not required, which simplifies the process for artisanal cheese production.

Thermodynamics characterization and potential textile applications of Trichoderma longibrachiatum KT693225 xylanase

Abstract Our study was a trial to participate in solving two main problems namely, environmental pollution resulting from accumulation and bad disposal of agro-industrial wastes, and high cost of industrial xylanase enzyme production. This was achieved through successful xylanase production by solid-state fermentation of low cost disposable agricultural wastes by marine fungal isolate Trichoderma longibrachiatum KT693225. The highest xylanase production 7.13 ± 0.11 U ml−1 was obtained utilizing rice straw (RS) waste after 7days of fermentation. Xylanase was purified by fractional precipitation with ethanol causing 4.24-fold purification. The 75% ethanol fraction was rich in cellulase, pectinase and α-amylase enzymes beside xylanase. The maximal xylanase activity was obtained at 60 °C, pH 5% and 2.5% xylan concentration. The Km and Vmax were calculated to be 20 mg ml−1 and 20 µmol min−1 ml−1, respectively. The thermostability of T.longibrachiatum KT693225 xylanase was indicated by low Ea (activation energy)and high Ed (energy of denaturation). High T1/2 (half life), D-value (decimal reduction time), ΔH° (enthalpy), ΔG° (free energy) and low Kd (denaturation rate constant), ΔS° (entropy) values at 70 °C emphasized high T.longibrachiatum KT693225 xylanase stability. T.longibrachiatum KT693225 xylanase showed high effectiveness at several textile wet-processing stages including desizing, bioscouring and biofinishing of cellulosic fabrics without adding any additives. These findings in this study have great implications for the future applications of xylanases.

Structural flexibility and protein adaptation to temperature: Molecular dynamics analysis of malate dehydrogenases of marine molluscs

Orthologous proteins of species adapted to different temperatures exhibit differences in stability and function that are interpreted to reflect adaptive variation in structural "flexibility." However, quantifying flexibility and comparing flexibility across proteins has remained a challenge. To address this issue, we examined temperature effects on cytosolic malate dehydrogenase (cMDH) orthologs from differently thermally adapted congeners of five genera of marine molluscs whose field body temperatures span a range of ∼60 °C. We describe consistent patterns of convergent evolution in adaptation of function [temperature effects on KM of cofactor (NADH)] and structural stability (rate of heat denaturation of activity). To determine how these differences depend on flexibilities of overall structure and of regions known to be important in binding and catalysis, we performed molecular dynamics simulation (MDS) analyses. MDS analyses revealed a significant negative correlation between adaptation temperature and heat-induced increase of backbone atom movements [root mean square deviation (rmsd) of main-chain atoms]. Root mean square fluctuations (RMSFs) of movement by individual amino acid residues varied across the sequence in a qualitatively similar pattern among orthologs. Regions of sequence involved in ligand binding and catalysis-termed mobile regions 1 and 2 (MR1 and MR2), respectively-showed the largest values for RMSF. Heat-induced changes in RMSF values across the sequence and, importantly, in MR1 and MR2 were greatest in cold-adapted species. MDS methods are shown to provide powerful tools for examining adaptation of enzymes by providing a quantitative index of protein flexibility and identifying sequence regions where adaptive change in flexibility occurs.

Purification and thermal denaturation kinetics of serum albumin in bactrian camel milk

Serum albumin is a non-specific transporter protein. It is the 2nd most abundant whey protein present in camel milk, with significantly higher content than in milk from other animals. In this study, we isolated and purified camel serum albumin (CSA) from milk by DEAE-Sepharose FF and Sephacryl S-100 gel filtration chromatography and checked its purity by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and ultra-performance liquid chromatography (UPLC). The main band of the purified product on SDS-PAGE corresponded with the location of a bovine serum albumin standard. In UPLC, the purified product presented a single sharp peak, which indicated it was a homogenous preparation. Amino acid sequence analysis of the purified protein confirmed it was CSA. Subsequently, we analysed the thermal denaturation of CSA from 70 to 95°C for 10, 20, 30, 40 and 50 min. CSA had upper stability under 75°C, the residual rate range over 70.25% to 87.12%. The degree of denaturation increased with temperature and time, but small range of fluctuations between denaturation rate. The residual rate of CSA, heated 10 min at 95°C, was about 58.34%. After CSA was heated 50 min at 95°C, it was not entirely denatured. These results suggested that CSA could maintain high stability in dairy products treated by low-temperature long-time or high-temperature short-time heating treatment and the reaction order of heat denaturation was 1.9. This study provides reference and application data for further research on CSA.

In vitro anti-inflammatory activity of Ficus racemosa L. bark using albumin denaturation method.

Introduction:In Ayurveda, many natural plant compounds are used to inhibit inflammatory pathways for centuries with less side effects. Different parts of Ficus racemosa L. (Udumber) plant are used in Ayurveda for many diseases. However, few studies have been conducted to evaluate pharmacological activities of F. racemosa.Objective:The objective of the study was to in vitro analyze anti-inflammatory property of F. racemosa bark using albumin denaturation activity.Methodology:F. racemosa bark extraction was performed using cold water and hot water. The concentration gradient of extracts was prepared using egg albumin and phosphate-buffered saline. The extract was incubated in a water bath at 37°C for 15 min and was heated at 70°C for 5 min. One nonsteroidal anti-inflammatory drug and one steroid were used as reference drugs. The percentage inhibition of protein denaturation was calculated.Results:The inhibition rate of egg albumin denaturation for water extraction increased gradually with concentration. Significantly higher inhibition was showed in hot water extracts than cold water extracts at the concentration of 0.01 μg/ml and 0.1 μg/ml. In addition, the inhibition rate of water extraction was significantly higher than the reference drugs (P < 0.05).Conclusion:Anti-inflammatory activity increases with the concentration of F. racemosa bark. Furthermore, the action of this plant is significantly higher than the reference drugs.