Effect of high-pressure treatment on the texture of cherry tomato

The effect of high-pressure treatment (200-600 MPa for 20 min) on the texture of cherry tomatoes and on the key softening enzymes (pectinmethylesterase and polygalacturonase) was investigated. When subjected to high-pressure treatment whole cherry tomatoes showed increasing textural damage with increasing pressures up to 400 MPa. However, treatment at pressures above 400 MPa (500-600 MPa) led to less apparent damage than treatment at 300 and 400 MPa; the tomatoes appearing more like the untreated samples. These visual changes were reflected in the texture (firmness) and amount of cell rupture in the tomatoes, with the least firmness and the most cell rupture being seen after treatment at 400 MPa. Light and scanning electron microscopy supported these observations. Although a sample of purified commercial pectinmethylesterase was partially inactivated at pressures above 200 MPa, irrespective of pH (4-9), in the whole cherry tomatoes no significant inactivation was seen even after treatment at 600 MPa, presumably because other components in the tomato offered protection or the isoenzymes were different. Polygalacturonase was more susceptible to pressure, being almost totally inactivated after treatment at 500 MPa. It is concluded that the textural changes in tomato induced by pressure involve at least two related phenomena. Initially, damage is caused by the greater compressibilty of the gaseous phase (air) compared to liquid-solid components, giving rise to a compact structure which, on pressure release, is damaged as the air rapidly expands, leading to increases in membrane permeability. This permits egress of water, and the damage also enables enzymatic action to increase, causing further cell damage and softening. The major enzyme involved in the further softening is polygalacturonase, which is inactivated at 500 MPa and above, and not pectinmethylesterase, which in the whole fruit, is barotolerant.     

Protective effect of ascorbic acid against the browning developed in apple fruit treated with high hydrostatic pressure.

Apple Reineta variety was used as an apple dessert. The 1-1.5-cm cubes were immersed in a sucrose solution (30% w/v) and subjected to high pressure (HP) of 400 MPa for 30 min at 5 degrees C. Different ascorbic acid concentrations were used to protect the fruit from the browning developed after the HP treatment. After 2 months of storage at 5 degrees C, no brown color was observed in the samples treated with 20 mM ascorbic acid, and they were acceptable to consumers. However, untreated samples presented fermentation, and they were not acceptable to consumers. The electric conductivity and potassium content were found to be good indicators of the metabolites released from the fruit to the solution in samples treated with high pressure. HP did not affect the peroxidase activity but eliminated the microbial population.     

Inactivation of apple pectin methylesterase induced by dense phase carbon dioxide

The inactivation of apple pectin methylesterase (PME) with dense phase carbon dioxide (DPCD) combined with temperatures (35-55 degrees C) is investigated. DPCD increases the susceptibility of apple PME to the temperatures and the pressures have a noticeable effect on apple PME activity. A labile and stable fraction of apple PME is present and the inactivation kinetics of apple PME by DPCD is adequately described by a two-fraction model. The kinetic rate constants k L and k S of labile and stable fractions are 0.890 and 0.039 min (-1), and the decimal reduction times D L and D S are 2.59 and 58.70 min at 30 MPa and 55 degrees C. Z T representing temperature increase needed for a 90% reduction of the D value and the activation energy E a of the labile fraction at 30 MPa is 22.32 degrees C and 86.88 kJ /mol, its Z P representing pressure increase needed for a 90% reduction of the D value and the activation volume V a at 55 degrees C is 21.75 MPa and -288.38 cm (3)/mol. The residual activity of apple PME after DPCD exhibits no reduction or reactivation for 4 weeks at 4 degrees C.     

Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L. Cv. italica).

Thermal and pressure inactivation of myrosinase from broccoli was kinetically investigated. Thermal inactivation proceeded in the temperature range 30-60 degrees C. These results indicate that myrosinase is rather thermolabile, as compared to other food quality related enzymes such as polyphenol oxidase, lipoxygenase, pectinmethylesterase, and peroxidase. In addition, a consecutive step model was shown to be efficient in modeling the inactivation curves. Two possible inactivation mechanisms corresponding to the consecutive step model were postulated. Pressure inactivation at 20 degrees C occurred at pressures between 200 and 450 MPa. In addition to its thermal sensitivity, the enzyme likewise is rather pressure sensitive as compared to the above-mentioned food quality related enzymes. By analogy with thermal inactivation, a consecutive step model could adequately describe pressure inactivation curves. At 35 degrees C, pressure inactivation was studied in the range between 0. 1 and 450 MPa. Application of low pressure (<350 MPa) resulted in retardation of thermal inactivation, indicating an antagonistic or protective effect of low pressure.     

超高压联合高密度CO2处理钝化对虾多酚氧化酶

为了弥补超高压(UHP,ultra high pressure)钝化凡纳滨对虾多酚氧化酶(PPO,polyphenol oxidase)效果差的缺点,同时利用高密度CO_2钝化凡纳滨对虾PPO的优势,初步研究UHP+CO_2处理对凡纳滨对虾PPO的钝化效果,以探讨UHP+CO_2联合处理用于开发虾类新产品的可行性。研究结果表明:UHP+CO_2联合处理比单独CO_2处理和UHP处理更能有效地钝化PPO;100 MPa UHP+CO_2联合处理30 min,PPO相对酶活降至18.92%±1.52%;200 MPa UHP+CO_2联合处理10 min,PPO相对酶活降至10.91%±1.08%;300 MPa UHP+CO_2联合处理10 min,PPO被钝化95%;400 MPa UHP+CO联合处理5 min,PPO被钝化97%;500 MPa UHP+CO联合处理10 min,PPO100%被钝化;与单独UHP处理相比,UHP+CO_2联合缩短了处理时间,提高了钝化PPO的效果;PPO经UHP+CO_2联合处理后在4℃贮藏6 d后活性未见恢复,说明PPO在处理过程中发生了不可逆的变性失活。研究结果为虾类的贮藏和加工以及开发新产品提供基础数据和技术参考。     

Structural changes of microbial transglutaminase during thermal and high-pressure treatment

The activity of microbial transglutaminase (MTG) and the corresponding secondary structure, measured by circular dichroism (CD), was analyzed before and after treatment at different temperatures (40 and 80 degrees C) and pressures (0.1, 200, 400, 600 MPa). Irreversible enzyme inactivation was achieved after 2 min at 80 degrees C and 0.1 MPa. Enzyme inactivation at 0.1, 200, 400, and 600 MPa and 40 degrees C followed first-order kinetics. The enzyme showed residual activity of 50% after 12 min at 600 MPa and 40 degrees C. Mobility of aromatic side chains of the enzyme molecule was observed in all temperature- and/or pressure-treated samples; however, high-pressure treatment at 600 MPa induced a loss of tertiary structure and a significant decrease in the alpha-helix content. The relative content of beta-strand substructures was significantly increased after 30 min at 600 MPa and 40 degrees C or 2 min at 0.1 MPa and 80 degrees C. We conclude that the active center of MTG, which is located in an expanded beta-strand domain, is resistant to high hydrostatic pressure and pressure-induced inactivation is caused by destruction of alpha-helix elements with a corresponding influence on the enzyme stability in solution.     

Denaturation of beta-lactoglobulin in pressure-treated skim milk

The kinetics of beta-lactoglobulin (beta-LG) denaturation in pressure-treated reconstituted skim milk samples over a wide pressurization range (100-600 MPa) and at various temperatures (10-40 degrees C) was studied. Denaturation was extremely dependent on the pressure and duration of treatment. At 100 MPa, no denaturation was observed regardless of the temperature or the holding time. At higher pressures, the level of denaturation increased with an increasing holding time at a constant pressure or with increasing pressure at a constant holding time. At 200 MPa, there was only a small effect of changing the temperature at pressurization. However, at higher pressures, increasing the temperature from 10 to 40 degrees C markedly increased the rate of denaturation. The two major genetic variants of beta-LG (A and B) behaved similarly to pressure treatment, although the B variant appeared to denature slightly faster than the A variant at low pressures (< or =400 MPa). The denaturation could be described as a second-order process for both beta-LG variants. There was a marked change in pressure dependence at about 300 MPa, which resulted in markedly different activation volumes in the two pressure ranges. Evaluation of the kinetic and thermodynamic parameters suggested that there may have been a transition from an aggregation-limited reaction to an unfolding-limited reaction as the pressure was increased.     

Unfolding and refolding of beta-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperatures and its influence on proteolysis

The unfolding of beta-lactoglobulin during high-pressure treatment and its refolding after decompression were studied by 1H NMR and 2H/1H exchange at pH 6.8 and 2.5 and at 37 and 25 degrees C. The extent of unfolding increased with the pressure level. The structure of beta-lactoglobulin required higher pressures to unfold at pH 2.5 than at pH 6.8. More flexibility was achieved at 37 degrees C than at 25 degrees C. Results indicated that the structural region formed by strands F, G, and H was more resistant to unfold under acidic and neutral conditions. The exposure of Trp19 at an earlier time, as compared to other protein regions, supports the formation of a swollen structural state at pH 2.5. Refolding was achieved faster when beta-lactoglobulin was subjected to 200 MPa than to 400 MPa, to 37 degrees C than to 25 degrees C, and to acidic than to neutral pH. After treatment at 400 MPa for 20 min at neutral pH, the protein native structure was not recovered. All samples at acidic pH showed that the protein quickly regained its structure. Hydrolysis of beta-lactoglobulin by pepsin and chymotrypsin could be related to pressure-induced changes in the structure of the protein. Compared to the behavior of the protein at atmospheric pressure, no increased proteolysis was found in samples with no increased flexibility (100 MPa, 37 degrees C, pH 2.5). Slightly flexible structures were associated with significantly increased proteolysis (100 MPa, 37 degrees C, pH 6.8; 200 MPa, 37 degrees C, pH 2.5). Highly flexible structures were associated with very fast proteolysis (>or=200 MPa, 37 degrees C, pH 6.8; >or=300 MPa, 37 degrees C, pH 2.5). Proteolysis of prepressurized samples improved only when the protein was significantly changed after the pressure treatment (400 MPa, 25 degrees C, 20 min, pH 6.8).     

Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of beta-lactoglobulin B

Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide). In the present study, beta-LG was mixed with sodium dodecyl sulfate (SDS), all-trans-retinol (retinol), or 8-anilino-1-naphthalenesulfonate (ANS) on a 1:1.1 molar basis, and aliquots were held at pressures between 50 and 800 MPa for 30 min at pH 7.2 and 20 degrees C. Polyacrylamide gel electrophoresis (PAGE) showed that beta-LG alone (control) was converted into a non-native monomer and a series of dimers, trimers, etc., at pressures beyond 100 MPa; SDS inhibited the formation of non-native species up to 200 MPa, and neither retinol nor ANS inhibited the formation of the non-native species as effectively as SDS. At pressures beyond 350 MPa, SDS ceased to have any inhibitory effect, but both ANS and retinol showed significant inhibition. The near- and far-UV CD patterns and the ANS fluorescent data were consistent with the PAGE data, but the retinol fluorescent data did not show sufficient change to interpret. The results suggested that there were three discernible structural stages. In Stage I (0.1-150 MPa), the native structure is stable; in Stage II (200-450 MPa), the native monomer is reversibly interchanging with non-native monomers and disulfide-bonded dimers; and in Stage III (>500 MPa), the free CysH in non-native monomer and dimer interacts with -S-S- bonds to produce high molecular weight aggregates of beta-LG. SDS inhibited the Stage I to Stage II transition at 200 MPa, and ANS and retinol inhibited the Stage II to Stage III transition at 600 MPa.     

Lipid globule staining to aid in differentiating Bacillus species.

The use of the lipid globule stain to aid in differentiating the Bacillus cereus group (i.e., B. cereus, B. cereus var. mycoides, and B. thuringiensis) from other Bacillus species was investigated. Smears from colonies grown on suitable agar were made on precleaned slides, stained, and examined microscopically for characteristic deep blue lipid globules. The study included a total of 649 cultures of Bacillus species plus 143 incompletely characterized Bacillus isolates from food. Only B. cereus, B. cereus var. mycoides, B. thuringiensis, B. megaterium, and B. sphaericus were consistently positive for lipid globules, although at times, a few cells of B. aneurinolyticus and B. thiaminolyticus were also positive. The lipid globule stain procedure is of value in differentiating Bacillus species, especially when performed by an experienced analyst and used in conjunction with tests for cell and spore morphology.     

A (1)H-NMR study on the effect of high pressures on beta-lactoglobulin

1H NMR was used to study the effect of high pressure on changes in the structure of beta-lactoglobulin (beta-Lg), particularly the strongly bonded regions, the "core". beta-Lg was exposed to pressures ranging from 100 to 400 MPa at neutral pH. After depressurization and acidification to pH 2.0, (1)H NMR spectra were taken. Pressure-induced unfolding was studied by deuterium exchange. Refolding was also evaluated. Our results showed that the core was unaltered at 100 MPa but increased its conformational flexibility at >/=200 MPa. Even though the core was highly flexible at 400 MPa, its structure was found to be identical to the native structure after equilibration back to atmospheric pressure. It is suggested that pressure-induced aggregates are formed by beta-Lg molecules maintaining most of their structure, and the intermolecular -SS- bonds, formed by -SH/-SS- exchange reaction, are likely to involve C(66)-C(160) rather than C(106)-C(119). In addition, the beta-Lg variants A and B could be distinguished in a (1)H NMR spectrum from a solution made with the AB mixed variant, by the differences in chemical shifts of M(107) and C(106); structural implications are discussed. Under pressure, the core of beta-Lg A seemed to unfold faster than that of beta-LgB. The structural recovery of the core was full for both variants.     

Changes in chymotrypsin hydrolysis of beta-lactoglobulin A induced by high hydrostatic pressure

Beta-lactoglobulin (beta-Lg) was subjected to high pressures up to 400 MPa and proteolysis with chymotrypsin. The hydrolysates were analyzed by SDS-PAGE and RP-HPLC, and the fragments obtained were identified by ESI-MS/MS. The results obtained showed that beta-Lg was hydrolyzed by chymotrypsin in a "progressive proteolysis" manner at either atmospheric or high pressure. Proteolysis during or after high-pressure treatment showed longer and more hydrophobic peptides than proteolysis at atmospheric pressure. Chymotrypsin showed a behavior similar to that of trypsin, with some differences, probably related to the orientation of the target residues specific for each enzyme. The similarities between proteolytic fragments produced by the two enzymes support that proteolysis enhancement under high pressure depends on the substrate changes rather than the enzyme. High pressure seemed to accelerate the first steps of proteolysis, probably through dimer dissociation, while leaving portions of the molecule more resistant to the enzyme.     

Tomato (Lycopersicon esculentum) pectin methylesterase and polygalacturonase behaviors regarding heat- and pressure-induced inactivation.

The combined high pressure/thermal (HP/T) inactivation of tomato pectin methyl esterase (PME) and polygalacturonase (PG) was investigated as a possible alternative to thermal processing classically used for enzyme inactivation. The temperature and pressure ranges tested were from 60 degrees C to 105 degrees C, and from 0.1 to 800 MPa, respectively. PME, a heat-labile enzyme at ambient pressure, is dramatically stabilized against thermal denaturation at pressures above atmospheric and up to 500-600 MPa. PG, however, is very resistant to thermal denaturation at 0.1 MPa, but quickly and easily inactivated by combinations of moderate temperatures and pressures. Selective inactivation of either PME or PG was achieved by choosing proper combinations of P and T. The inactivation kinetics of these enzymes was measured and described mathematically over the investigated portion of the P/T plane. Whereas medium composition and salinity had little influence on the inactivation rates, PME was found less sensitive to both heat and pressure when pH was raised above its physiological value. PG, on the other hand, became more labile at higher pH values. The results are discussed in terms of isoenzymes and other physicochemical features of PME and PG.     

High-pressure effects on the proteolytic enzymes of sea bass (Dicentrarchus labrax L.) fillets

High-pressure processing is a nonthermal technique ensuring food product safety and enabling a longer shelf life. The purpose of this experiment was to evaluate the effect of high pressure on the main proteolytic enzymes involved in fish muscle degradation during storage. Enzymes were extracted with sarcoplasmic proteins from Dicentrarchus labrax sea bass white muscle. Activity of cathepsins B, D, H, and L was quantified in protein extract, whereas calpain activity was evaluated after isolation from its endogenous inhibitor. High-pressure processing up to 500 MPa enhanced the activity of cathepsin B, H, and L, whereas the activity of cathepsin D increased up to 300 MPa and decreased above 300 MPa. With regard to calpain activity, high-pressure processing led to a decrease of activity, which was zero above 400 MPa. We suggest a leading explanation based on simultaneous deactivation of enzymes and an increase of liberation from lysosomes for cathepsins and on dissociation of subunits for calpains.     

Effect of high-pressure treatment on lipoxygenase activity

Solutions of commercial soybean lipoxygenase (100 microgram/ML in 0.2 M citrate-phosphate and 0.2 M Tris buffer were subjected to pressures of 0.1, 200, 400, and 600 MPa for 20 mm. The enzyme was stable at atmospheric pressure (0.1 MPa) over a wide pH range (5-9). In citrate phosphate buffer, the enzyme had maximum stability over the pH range 58 in untreated samples and after treatment at 200 MPa, but with increasing pressure, the pH stability range become narrower and centered around pH 78. The enzyme was more sensitive to acid than alkali, and at pH 9, it lost virtually all activity after pressurization at 600 MPa for 20 mm in both buffers. The activity of the crude enzyme extracted from tomatoes treated at 200 and 300 MPa for 10 mm was not significantly different from that of the untreated tomatoes, while a pressure of 400 MPa for 10 mm caused a significant decrease in activity and treatment at 600 MPa led to complete and irreversible activity loss. Compared to unpressurized tomatoes, treatment at 600 MPa gave significantly reduced levels of hexanal, cis-3-hexenal, and trans-2-hexenal, which are important contributors to "fresh" tomato flavor, and this was attributed to the inactivation of lipoxygenase.     

超高压辅助脱壳处理对泥蚶肉品质的影响

为研究超高压对泥蚶脱壳率及其肌肉品质的影响,以鲜活泥蚶为材料,初步确定合适的辅助泥蚶脱壳的超高压处理参数,并在这些参数条件下,考察超高压对泥蚶肌肉色差、质构、菌落总数和氨基酸组成及其营养评价的影响。结果表明,泥蚶经300 MPa保压5 min(300/5),350 MPa分别保压3、5 min(350/3、350/5),或400 MPa保压1 min(400/1)处理,其脱壳率均达到100%,同时具有较高感官质量。在上述4组优化参数下,超高压组泥蚶肉的白度较对照组显著提高,但超高压组间的总色差值无显著差异;其硬度值提高,黏附性、弹性、内聚性和恢复度值均有所减少;泥蚶的菌落总数从5.3×10⁴ CFU·g^-1 降至10~100 CFU·g^-1;泥蚶肉氨基酸总量随压力增加而逐渐降低,其中400/1组色氨酸未检出,氨基酸总量比新鲜泥蚶肉下降7.58%,且除400/1组外,其余组泥蚶肉的蛋白均为优质蛋白。传统漂烫、超高压处理均不改变泥蚶肉第一、第二限制性氨基酸种类,分别为甲硫氨酸和色氨酸。综合超高压处理对泥蚶脱壳及泥蚶肉品质的影响,合适的工艺参数为300 MPa保压5 min以及350 MPa保压3~5 min。本研究结果为超高压脱壳技术在泥蚶加工中的应用提供了一定的理论指导。     

Use of fatty acid profiles to identify food-borne bacterial pathogens and aerobic endospore-forming bacilli

Capillary gas chromatography (GC) with flame ionization detection was used to determine the cellular fatty acid profiles of various food-borne microbial pathogens and to compare the fatty acid profiles of spores and vegetative cells of the same endospore-forming bacilli. Fifteen bacteria, representing eight genera (Staphylococcus, Listeria, Bacillus, Yersinia, Salmonella, Shigella, Escherichia, and Vibrio) and 11 species were used to compare the extracted fatty acid methyl esters (FAMEs). Endospore-forming bacilli were processed to obtain pure spores and whole cell FAMEs for GC analysis. A data set for each bacterial agent was prepared using fatty acid profiles from five replicates prepared on different days. The results showed that these fatty acid intensity profiles were unique for each of the 11 species and that they could be used as a fingerprint for the organisms. The cellular fatty acid profiles for Bacillus anthracis and Bacillus cereus show that there are two branched chain fatty acids, iso 17:1 omega10c and 17:1 anteiso, which are unique in these species. Iso 17:1 omega10c is present in B. cereus vegetative cells and spores but is not observed in B. anthracis. The 17:1 anteiso fatty acid is present in B. anthracis cells but not in B. cereus cells. Fatty acids 16:0 2OH and 17:0 iso 3OH are present in B. anthracis and B. cereus spores but not in the vegetative cells. In summary, analysis of FAMEs from bacteria and spores can provide a sensitive procedure for the identification of food-borne pathogens.     

蜡样芽孢杆菌及其生物被膜对有机酸及乙醇的抗性比较

为比较蜡样芽孢杆菌及其生物被膜对环境压力的抗性,该文主要研究了4种有机酸（乙酸、柠檬酸、乳酸和苹果酸）和乙醇对蜡样芽孢杆菌及其生物被膜存活率的影响。结果表明：生物被膜态蜡样芽孢杆菌对乙酸的抗性高于浮游态菌。扫描电镜结果显示,经乙酸处理后,浮游态蜡样芽孢杆菌的细胞表面严重受损,而生物被膜态菌的表面形态未发生明显变化。在柠檬酸、乳酸、苹果酸和乙醇存在的条件下,生物被膜态蜡样芽孢杆菌比浮游态菌表现出更强的压力抗性,特别是在高浓度（有机酸16%～20%,乙醇50%～60%）的情况下,该现象尤为显著。因此,在食品工业中控制被膜态蜡样芽孢杆菌对预防和阻止食品腐败非常重要。该研究结果为实际生产中有效控制蜡样芽孢杆菌及其生物被膜的形成提供参考。     

Effect of ultrahigh hydrostatic pressure on the activity and structure of mushroom (Agaricus bisporus) polyphenoloxidase

High hydrostatic pressure (HHP, treatment pressure ≤700 MPa) is approved to be the most successful commercial nonthermal processing due to its minimal modifications in nutritional and sensory quality. However, for some pressure stable enzymes such as PPO, this unique technology can hardly inactivate them at treatment pressure below of 700 MPa. This study investigated the effects of ultrahigh hydrostatic pressure (UHHP, treatment pressure >700 MPa) on the activity of Agaricus bisporus mushroom polyphenoloxidase (PPO) both in the phosphate buffer and in the mushroom puree, and on the structure of the enzyme by means of circular dichroism (CD), fluorescence emission spectra, and sulphydryl group detection. The results showed that UHHP treatment at pressure from 800 to 1600 MPa caused significant inactivation on the PPO both in the phosphate buffer and in the mushroom puree. UHHP treatment at 1400 and 1600 MPa for 1 min reduced the enzyme activity by 90.4% and 99.2% in the buffer;, however, higher enzyme activity remained in the puree after UHHP treatment at the same condition. CD and fluorescence spectra analysis showed that the secondary and tertiary structures of UHHP treated mushroom PPO were changed. The sulphydryl group (SH) detection revealed that the SH content on the surface of UHHP treated mushroom PPO was increased. It has been suggested that the inactivation of mushroom PPO by UHHP treatment at pressure higher than 1000 MPa was due to the synergistic effect of the pressure and the heat arising from pressurization, in which heat plays a major role.     

超高压加工鲜切苹果片的色变动态特性

以红富士和冰糖心2种苹果为试材,研究0、200、300、400和500MPa超高压处理对鲜切苹果片的色变动态特性。结果表明,超高压处理能显著抑制鲜切苹果片在空气中的色变速率。采用4种三色值组合(ΔL*a*/b* 、ΔL*a*b*、Δ(ΔE)和ΔW.I.)作为色变指标研究鲜切苹果片的色变动态特性,结果表明,超高压处理和未处理的鲜切苹果片的各色变指标均随时间呈线性变化,鲜切苹果片的色变符合零级动力学反应。通过对三色值组合的优选,色变指标ΔL*a*/b*被选作反应压力对色变影响的最佳指标,并在此基础上建立了色变指标(ΔL*a*/b*)与压力(P)的关系模型。模型表明,400MPa为超高压加工鲜切水果片的较优压力。