respuesta de banano al frío

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Postharvest Biology and Technology 55 (2010) 154159

Contents lists available at ScienceDirect

Postharvest Biology and Technology

j o u r n a l h o m e p a g e : w w w . e l s e v i e r . c o m / l o c a t e / p o s t h a r v b i o

Physiology and quality response of harvested banana fruit to cold shock

Haiyan Zhang a, Shaoyu Yang a, Daryl C. Joyce b, Yueming Jiang a, Hongxia Qu a, Xuewu Duan a,

a South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, PR Chinab The University of Queensland, School of Land, Crop and Food Sciences, Gatton, Qld. 4343, Australia

a r t i c l e i n f o

Article history:

Received 29 July 2009

Accepted 14 November 2009

Keywords:

Banana

Cold shock treatment

Postharvest life

Softening

Ethylene

a b s t r a c t

Experiments were conducted to examine softening and quality responses of harvested banana fruit to

cold shocktreatment intended to extendshelf-life. Fruit were immersed in ice-water for1 h, then treated

withorwithout100

L L1 ethylenefor24hat24 C,andfinallystoredat20 C. Fruitfirmness, chlorophyll

content, ethylene production, respiration rates, contents of pectin, starch and sugar, and the activities of

the cell wall modifying enzymes polygalacturonase (PG), pectin methylesterase (PME) and CMCase (cel-

lulase, endo-1,4--glucanase) were analyzed. Total amylase activity was also measured. Immersion inice-water for 1 h effectively inhibitedripening-associated processes, including peelde-greening andpulp

softeningduring storage or ripening.The delay in ripening wasalso manifestin reduced ethylene produc-

tionand respiration rates. Theinhibition of softeningby coldshock treatmentwas related to decreasedPG

and PME activities, that is, retardation of pectin solubilization/degradation. Reduced activitiesof CMCase

andtotalamylase and conversion of starchto sugar by ice-waterimmersion also contributed to thedelay

in softening of harvested banana fruit.

2009 Elsevier B.V. All rights reserved.

1. Introduction

Banana is a typical climacteric fruit characterized by a pre-climacteric phase followed by a peak in ethylene production

that co-ordinates ripening-associated process, including climac-

teric respiration, pulp softening, peel de-greening, and production

of aroma compounds(Clendennen andMay, 1997). The physiologi-

cal climacteric attributeof banana fruit leads to a short postharvest

life of 1015 d at ambient temperature. In developing countries, it

is estimatedthat 2030%of thefruitis lost after harvest dueto poor

handling and storage (Li and Jia, 2008).

Banana handling, transportation, and marketing, including gas

ripening, typicallyinvolve sophisticated technologies and facilities.

Approaches such as cold and controlled atmosphere (CA) storage

arevery efficient in extendingshelf-life of harvestedbananas (Scott

and Soertini, 1974). In developed countries, bananas are typically

cooled to13

C for storage and transport. Slowed fruitmetabolismdelays the onset of ripening andsenescence. CA storage can further

extend shelf-life of fruit by incrementally decreasing metabolism

and suppressing decay. For mature green bananas, low oxygen

concentrations (e.g. 2.5% O2) reduce respiration, peel de-greening

and starch and sugar conversions (Kanellis et al., 1989), and also

minimise susceptibility to crown rot (Marchal, 1998). However,

application of cold storage and CA is prohibitively high cost in

Corresponding author. Tel.: +86 20 37252960; fax: +86 20 37252831.

E-mail address: [email protected] (X. Duan).

developing countries, and alternative, less sophisticated low cost

technologies without refrigeration, are needed.

Recent research indicates that short-term rapid cooling bycold air or ice-water can extend shelf-life and improve quality

of some fruit (Alique et al., 2005; Barry and van Wyk, 2006).

Coldshock treatmentshave beenshown to delayripening-related

colour development and softening of harvested tomato (Inaba and

Crandall,1986; Shao et al., 2002) andloquat (XuandXu,2001) fruit.

In a preliminary study, short-term cold air treatment delayed soft-

ening of banana fruit at 24 C. However, there is a need to better

understand effects of cold shock treatment on ripening processes

in harvested fruit, including banana.

The objective of this study was, therefore, to elucidate effects of

cold shock on biochemical and physiological changes in harvested

banana fruit with a view to future optimization of this postharvest

technology for green life extension.

2. Materials and methods

2.1. Plant material

Hands of mature green banana (Musa spp., AAA group cultivar

Brazil)were obtained from a local farm in Guangzhou. Hands were

cut into fingers, and dipped for 3 min in 0.1%Sportak (a.i. prochlo-

raz, Bayer) fungicide solution to control postharvest diseases, and

then allowed to air-dry. Fruit were selected forfreedom from visual

defects and uniformity of shape, colour and size.

0925-5214/$ see front matter 2009 Elsevier B.V. All rights reserved.

doi:10.1016/j.postharvbio.2009.11.006
http://www.sciencedirect.com/science/journal/09255214http://www.elsevier.com/locate/postharvbiomailto:[email protected]://dx.doi.org/10.1016/j.postharvbio.2009.11.006http://dx.doi.org/10.1016/j.postharvbio.2009.11.006mailto:[email protected]://www.elsevier.com/locate/postharvbiohttp://www.sciencedirect.com/science/journal/09255214


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H. Zhang et al. / Postharvest Biology and Technology 55 (2010) 154159 155

2.2. Treatments

2.2.1. Preliminary experiments

Preliminary small-scale experiments were conducted to deter-

mine relative effects of various treatment durations and temper-

atures with cold air or ice-water on the green life of harvested

banana fruit. Thirty fruit were placed into a low temperature-

controlled cabinet (5 C; 125 L; fan forced air circulation) for 1.5,

3 or 4.5 h. For ice-water treatment, 30 banana fruit were dipped

into 50L of ice-water (ratio of ice to water= 6:4) for 0.5, 1 or 2 h.

After treatments with cold air or ice-water, fruit were removed

from the temperature-controlled cabinet or ice-water, allowed to

stabilize for 3 h at room temperature (25 C), and packed into

0.03mm thick low density polyethylene bags (LDPE; 3 fruit per

bag), and then stored at 20 C. Fruit without cold shock treatment

were controls. During storage, green life was evaluated according

to changes of firmness andcolour.Results (datanot shown)showed

that immersionin ice-waterfor 1 h gave greatest extensionin green

life of banana fruit. Thus, this treatment was used in subsequent

experiments.

2.2.2. Effects of cold shock treatments on biochemical and

physiological changes

In this experiment, bananafruit were immersed in ice-waterfor1 h as above.Fruitinteriortemperatures were loggedby a computer

and thermocouples system. After cold shock treatment, fruit were

allowed toequilibratefor 3 h atroomtemperature, andthenpacked

into 0.03mm thick LDPE bags (3 fruit per bag). Thereafter, fruit

were held at 20 C and sampled for biochemical and physiological

analyses at 5, 10, 15, 20 and 25 d of storage.

2.2.3. Cold shock and ethylene treatments

Cold shock treatment was conducted as above. After this treat-

ment, banana fruit were treated with 100L L1 ethylene in sealedjars for 24h at24C. Thereafter, fruit were held at 20 C and 90% rel-

ative humidity (RH) to evaluate shelf-life and analyze physiological

and biochemical changes at 3, 5 and 7 d of storage.

2.3. Ethylene production and respiration rate

Three fruit were sealed inside a 4.2 L glass jar for 2 h at 20 C.

One milliliter aliquots of headspace gas were withdrawn from

the jars and injected into a gas chromatograph (GC-9A; Shi-

madzu, Kyoto, Japan). Carbon dioxide (CO2) concentrations were

determined using a thermal conductivity detector (TCD) and a

Poropak N column (Shimadzu). Ethylene concentrations were mea-

sured using a flame ionisation detector (FID) and an HP-PLOT Q

capillary column (Agilent Technologies, USA). Rates of ethylene

production and respiration were expressed on a fresh weight (FW)

basis.

2.4. Fruit firmness

Peel tissues from one side of banana fingers were removed

and pulp firmness measurements taken at three different points

using a penetrometer (Model GY-1, Hangzhou Scientific Instru-

ments, Hangzhou, China) fitted with a 3.5 mm diameter flat probe.

Penetration force was recorded as N for the flat probe area.

2.5. Chlorophyll content

Peel discs were removed with a cork borer (10 mm diameter)

from one side of banana fingers. Twenty discs were ground with

liquid nitrogen, extracted for 30 min with 20 mL of 80% acetone

(v/v) in the dark, and then centrifuged at 3000 g for 10min.

The supernatant was used to determine the chlorophyll content

spectrophotometrically according to the method of Lichtenthaler

(1987).

2.6. Contents of total soluble sugar, starch and pectins

Starch content in the pulp was measured according to the

method described by Azelmat et al. (2006), and total soluble

sugar was determined using the anthrone method (Yemm and

Willis, 1954). Water soluble pectin (WSP) and acid soluble pectin(ASP) were extracted according to the method of Cheng et al.

(2008). Uronic acid concentrations in WSP and ASP fractions were

measured by the m-hydroxydiphenyl method (Blumenkrantz

and Asboe-Hansen, 1973) using galacturonic acid (GA)

standards.

2.7. Extraction and assay of cell wall degrading enzymes

Five grams of pulp from banana fruit was homogenized with

20 mL of 50 mM sodium acetate buffer (pH 4.5) containing 7.5%

(w/v) NaCl and 0.5g of polyvinylpyrrolidone (insoluble) at 4 C.

The homogenate was centrifuged at 10,000gfor 20min and the

supernatant used for assaying the activities of polygalacturonase

(PG) and CMCase (cellulase).To measure PG activity, the supernatant was dialyzed overnight

in 50 mM sodium acetate buffer (pH 4.5). The reaction mixture

contained 0.4 mL of 200mM sodium acetate (pH 4.5), 0.3mL of

polygalacturonic acid (PGA, 1% aqueous solution adjusted to pH

4.5), 0.2mL of distilled water, and 0.1 mL of dialyzed enzyme

extract. The reaction was initiated by addition of the PGA sub-

strate. The mixture was incubated at 37 C for 1h, followed by

addition of 3,5-dinitrosalicylate (DNS) reagent. The reaction was

terminated by heating the reaction mixture in a boiling water

bath for 5 min. In control tubes the substrate was added after the

heat treatment. The formation of reducing groups was estimated

using DNS reagent against galacturonic acid (GalA) standards

(Luchsinger and Cornesky, 1962). PG activity was expressed as

gGalAmg1 protein min1.Enzymes which may be involved in matrix glycan depoly-

merization are mainly the endo-1,4--glucanase (EGases), whichhydrolyse internal 1,4--glucanlinkages. Activity is usually mea-sured in vitro against the model substrate carboxymethylcellulose

(CMC) (Harpster et al., 2002). In this study, EGase was assayed

using CM-cellulose as substrate and termed as CMCase activ-

ity. The amount of reducing sugar released was determined

using DNS reagent, against glucose (Glu) as the standard

(Luchsinger and Cornesky, 1962). CMCase activity was expressed

as gGlumg1 protein min1.Pectin methylesterase (PME) activity was measured accord-

ing to the method of Hangermann and Austin (1986) with some

modification. Five grams of pulp was ground with 20 mL of 8.8%

(w/v) NaCl and 0.5g of polyvinylpyrrolidone (insoluble) at 4

C.The homogenate was centrifuged at 10,000g for 30min. The

supernatant was collected, adjusted to pH 7.5 and assayed for PME

activity. The activity was assayed in a mixture containing 2.0mL of

0.5% (w/v) pectin, 0.15mL of 0.01% bromothymol blue, 0.75 mL of

water,and 0.1mL of enzyme extract. Allsolutions (pectin, indicator

dye, water)were adjusted to pH 7.5with 2 M NaOH just beforeeach

trial was started. After adding the enzyme extract, the decrease in

the absorbance at 620 nm was measured spectrophotometrically.

Calculation of the activity was carried out against the standard

curve as describedby Hangermann and Austin (1986). PME activity

was expressed as molGalAmg1 protein min1.Protein contents were determined according to the method

of Bradford (1976), with bovine serum albumin as the

standard.
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156 H. Zhang et al. / Postharvest Biology and Technology 55 (2010) 154159

Fig. 1. Effects of cold shock treatment on pulp firmness (A), peel chlorophyll content (B), respiration rate (C) and ethylene production rate (D) of banana fruit during storage

at 20 C. Each data point represents a mean standard error (n =3).

2.8. Extraction and assay of total amylase activity

Five grams of pulp was homogenized with 20 mL of 100 mM

HEPES-KOH buffer (pH 7.0) containing 0.3% (w/v) NaCl, 20 mM

cysteine, 1 mM benzamidine, and 0.5g of polyvinylpyrrolidone

(insoluble) at 4 C. After centrifugation at 12,000g for 40min,

the crude extracts were immediately used for assays. Total amy-

lase activities were assayed as described by Bernfeld (1955) with

1% (w/v) starch solution in 100 mM acetate buffer (pH 5.9). Forma-tion of reducing groups was estimated against maltose (Mal) as the

standard by measurements of absorbance at 540nm. Total amylase

activity was expressed as gMalmg1 protein min1.

2.9. Data handling

Experiments were arranged in a completely randomised design

with three replicates. Treatments were compared by analysis of

variance using SPSS version 7.5 (SPSS Inc., Chicago, IL, USA). Least

significant differences(LSD) were calculatedto compare significant

treatment effects at P


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Table 1

Effect of ice-water immersion for 1 h on contents of water soluble pectin (WSP), acid soluble pectin (ASP), starch and total soluble sugar (TSS) of banana fruit during storage

at 20 C. Each data point represents a mean standard error (n = 3). Means in a row with the same letter for each parameter were not significantly different at P


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158 H. Zhang et al. / Postharvest Biology and Technology 55 (2010) 154159

Fig. 3. Changes in pulp firmness (A), peel chlorophyll content (B), respiration rate (C) and ethylene production rate (D) of harvested banana fruit treated with or without

ice-water for 1h followed by treatment with 100L L1 ethylene for 24h, and then allowed to ripen at 20 C. Each data point represents a meanstandard error (n =3).

Similarly, softening of banana fruitafter ethylene treatment was

accompanied by a decrease in ASP content and increase in WSP

content associated with increased PG and PME activities. Markedly

reduced but similar patterns in ASP and WSP contents and in PG

activitywere observed whenfruit weretreatedwith ice-water prior

to ethylene treatment(Table 2 and Fig.4A). ForPME,activityin fruit

treated with ice-water was also lower than that in control fruit

after 5 d of ripening. Inhibition of PG and PME activities and pectindegradation by cold shock treatment prior to ethylene treatment

show that cold shock treatment restricted induction of PG and PME

activities by ethylene.

Inhibition of conversion of starch to sugar after ethylene treat-

ment by cold shock treatment might also contribute to the delay

in fruit softening. On the fifth day, contents of starch and total sol-

uble sugars in ice-water-treated fruit prior to ethylene treatment

were 196% and 76%, respectively, of those in control fruit (Table 2).

Moreover, ice-water-treated fruit hada much lower total amylases

activity than control fruit (Fig. 4C).

As cold shock treatment delayed banana fruit ripening induced

by ethylene, it is proposed that cold acts in part at least by inter-

fering with ethylene perception or signal transduction. Delayed

fruit ripening upon cold shock treatment might involve differen-tial regulation of gene expression. Bae et al. (2003) found that

54 nuclear proteins in Arabidopsis were up- or down-regulated

greater than 2-fold in response to cold shock treatment at 4 C

for 6 h. Similarly, transcripts of 53 genes in Arabidopsis increased

more than 5-fold compared with control genes after cold shock

treatment (Seki et al., 2002). Sangwan et al. (2002) suggest that

cold is sensed by structural changes in the plasma membrane that

transducesthe signalvia the cytoskeleton, Ca2+ fluxes, and calcium-

dependent protein kinases (CDPKs), which leads to activationof distinct mitogen-activated protein kinases (MAPKs) cascades.

Such cascades could bring about pronounced alterations in gene

expression.

In conclusion, treatment with 0 C ice-water for 1 h effectively

inhibited peel de-greening and pulp softening of harvested banana

fruit during storage or ripening and thereby extended green life

or shelf-life of the fruit. The delayed ripening was also mani-

fest in reduced ethylene production and respiration rates. Cold

shock treatment reduced PG and PME activities and slowed down

pectin solubilization/degradation, which resulted in inhibition of

fruit softening. The delay in fruit softening was also related to

reduced EGase and total amylase activities. As a simple and inex-

pensive postharvest technology, utilisation of cold shock treatment

to manipulate fruit physiology and biochemistry is a practicalapproach to extending the green life of bananas.

Table 2

Changes in contents of water soluble pectin (WSP), acid soluble pectin (ASP), starch and total soluble sugar (TSS) of harvested banana fruit treated with or without ice-water

for 1 h followed by treatment with 100L L1 ethylene for 24h, and then allowed to ripen at 20 C. Each value was presented as a mean standard error (n = 3). Means in a

row with the same letter for each parameter were not significantly different at P


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Fig. 4. Changes in activities of polygalacturonase (PG) (A), pectin methyl esterase

(PME) (B), and total amylase (C) of harvested banana fruit treated with or without

ice-water for 1 h followed by treatment with 100L L1 ethylene for 24h, and then

allowed to ripenat 20C.Eachdatapointrepresentsa meanstandarderror (n =3).

Acknowledgments

This work was supported by the International Foundation for

Science (Grant No. E/3656-1), the National Natural Science Founda-

tion of China(Grant Nos.30500353 and U0631004) and Guangdong

Provincial Science Foundation of China (Grant No. 06200670).

References

Ali,Z.M.,Chin, L.H.,Lazan,H., 2004. A comparativestudy onwall degradingenzymes,pectin modifications and softening during ripening of selected tropical fruits.Plant Sci. 167, 371-327.

Alique, R., Zamorano, J.P., Martynez, M.A., Alonso, J., 2005. Effect of heat and coldtreatments on respiratorymetabolismand shelf-life of sweet cherry, typepicotacv Ambrunes. Postharvest Biol. Technol. 35, 153165.

Asif, M.H., Nath, P., 2005. Expression of multiple forms of polygalacturonase geneduring ripening in banana fruit. Plant Physiol. Biochem. 43, 177184.

Azelmat, K., ELGarrouj, D., Mouhib, M., Sayah, F., 2006. Irradiation of Boufeggousdates: effectson chemicalcompositionduring storage.PostharvestBiol. Technol.39, 217222.

Bae, M.S., Cho, E.J., Choi, E.Y., Park, O.K., 2003. Analysis of the Arabidopsis nuclearproteome and its response to cold stresses. Plant J. 36, 652663.

Barry, H.B., van Wyk, A.A., 2006. Low-temperature cold shock may induce rind

colour development of Nules Clementine mandarin ( Citrus reticulata Blanco)fruit. Postharvest Biol. Technol. 40, 8288.

Bernfeld, P., 1955. Amylase, alpha and beta. Methods Enzymol. 1, 149158.Blumenkrantz, N., Asboe-Hansen, G., 1973. New method for quantitative determi-

nation of uronic acids. Anal. Biochem. 54, 484489.Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of micro-

gram quantities of protein utilizing the principle of protein-dye binding. Anal.Biochem. 72, 248254.

Brummell, D.D., Harpster, M.H., 2001. Cell wall metabolism in fruit softening andquality and its manipulation in transgenic plants. Plant Mol. Biol. 47, 311340.

Chang, W.H., Hwang, Y.J., 1990. Effect of ethylene treatment on the ripen-ing, polyphenoloxydase activity and water soluble tannin content of Taiwannorthern banana at different maturity stages and the stability of bananapolyphenoloxydase. Acta Hortic. 275, 603610.

Cheng, G.P., Duan, X.W., Yang, B., Jiang, Y.M., Lu, W.J., Luo, Y.B., Jiang, W.B., 2008.Effect of hydroxylradicalon the scission of cellular wallpolysaccharidesin vitroof banana fruit at various ripening stages. Acta Physiol. Plant. 30, 257263.

Clendennen, S.K., May, G.D., 1997. Differential gene expression in ripening bananafruit. Plant Physiol. 155, 463469.

do Nascimento, J.R.O., Junior, A.V., Bassinello, P.Z., Cordenunsi, B.R., Mainardi, J.A.,2006.Beta-amylase expression and starch degradation during banana ripening.Postharvest Biol. Technol. 40, 4147.

Hangermann, A.E., Austin, P.J., 1986. Continuous spectrophotometric assay for plantpectin methyl-esterase. J. Agric. Food Chem. 34, 440444.

Harpster, M.H., Brummell, D.A., Dunsmuir, P., 2002. Suppression of a ripening-related endo-1,4--glucanase in transgenic pepper fruit does not preventdepolymerization of cell wall polysaccharides during ripening. Plant Mol. Biol.50, 345355.

Harpster, M.H., Lee,K.Y., Dunsmuir, P.,1997. Isolationand characterization of a geneencoding endo--1,4-glucanase from pepper (Capsicum annuum L.). Plant Mol.Biol. 33, 4759.

Inaba, M., Crandall, P.G., 1986. Cold-shock treatment of mature green tomatoes todelaycolor development and increase shelf life during room temperature.Proc.Florida State Hortic. Soc. 99, 143145.

Kanellis,A.K., Solomos,T., Mattoo,A., 1989. Changesin sugar, enzymic activitiesandacid phosphatase isoenzyme profiles of banana ripened in air or stored in 2.5%O2 with and without ethylene. Plant Physiol. 90, 251258.

Li, Y., Jia, F., 2008. A survey on status and countermeasures of banana industry inChina. Chinese Agric. Sci. Bull. 24, 443447 (in Chinese with English abstract).Lichtenthaler, H.K.,1987.Chlorophylls andcarotenoids:pigments of photosynthetic

biomembranes. Methods Enzymol. 148, 350382.Luchsinger, W.W., Cornesky, R.A., 1962. Reducing power by the dinitrosalicylic acid

method. Anal. Biochem. 4, 346347.Marchal, J., 1998. An overview of post-harvest aspects of banana. Acta Hortic. 490,

501510.Prasanna, V., Prabha, T.N., Tharanathan, R.N., 2007. Fruit ripening phenomena an

overview. Crit. Rev. Food Sci. 47, 119.Sangwan,V., Orvar, B.L.,Beyerly, J., Hirt,H., Dhindsa,R.L., 2002. Oppositechangesin

membrane fluidity mimic cold and heat stress activation of distinct plant MAPkinase pathways. Plant J. 31, 629638.

Scott, K.J., Soertini,G., 1974. Effect of temperatureon thestoragelife of bananasheldin polyethylene bags with an ethylene absorbent. Trop. Agric. 51, 2326.

Seki,M., Narusaka,M., Ishida,J., Nanjo, T.,Fujita,M., 2002. Monitoringthe expressionprofilesof 7000Arabidopsis genes under drought,coldand high-salinitystressesusing a full-length cDNA microarray. Plant J. 31, 279292.

Shao, Z.P.,Ying,T.J.,Wang,Y.G.,2002.Effectsof coldshock onpostharvestphysiology

of tomato. J. Nanjing Agric. Univ. 25, 97100 (in Chinese with English abstract).Vicente, A.R., Costa, M.L., Martynez, G.A., Chaves, A.R., Civello, R.M., 2005. Effect

of heat treatments on cell wall degradation and softening in strawberry fruit.Postharvest Biol. Technol. 38, 213222.

Xu, Y., Xu, C., 2001. Effect of cold shock on PG activity of harvested loquat. Jiansu J.Agric. Sci. 17, 127128 (in Chinese with English abstract).

Yemm, E.W., Willis, A.J., 1954. The estimation of carbohydrates in plant extracts byanthrone. New Phytol. 57, 508512.

respuesta de banano al frío

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