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Jan 1, 2018 - crobial colonies of the watermelon juice (Zhang, Wang, Ma, Zhao, & Li, ... 2009), cucumber juice (Liu, Zhang, Zhao, Wang, & Liao, 2016), and.
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Received: 7 September 2017    Revised: 7 November 2017    Accepted: 1 January 2018 DOI: 10.1002/fsn3.593

ORIGINAL RESEARCH

Effect of ultrahigh temperature treatment on qualities of watermelon juice Yubin Wang1,2,3 | Xiaofei Guo2,3 | Yue Ma1,2,3 | Xiaoyan Zhao1,4 |  Chao Zhang1,2,3 1 Beijing Vegetable Research Center, Beijing Academy of Agriculture and Forestry Sciences, Beijing, China 2

Abstract The watermelon juice was pasteurized by the ultrahigh temperature (UHT) treatment,

Beijing Key Laboratory of Fruits and Vegetable Storage and Processing, Ministry of Agriculture, Beijing, China

and the qualities of the pasteurized juice were compared to screen the optimal UHT.

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original color of the watermelon juice. The temperature of 120 and 135°C was also

Key Laboratory of Vegetable Postharvest Processing, Ministry of Agriculture, Beijing, China 4 Key Laboratory of Biology and Genetic Improvement of Horticultural Crops (North China), Ministry of Agriculture, Beijing, China

Correspondence Chao Zhang, Beijing Vegetable Research Center, Beijing Academy of Agriculture and Forestry Sciences, Beijing, China. Email: [email protected] Funding information Natural Science Foundation of Beijing Municipality, Grant/Award Number: 6172013; China Agricultural Research System, Grant/ Award Number: CARS-25; Beijing Key Laboratory of Fruits and Vegetable Storage and Processing, Grant/Award Number: Z141105004414037; Beijing Academy of Agricultural and Forestry Sciences, Grant/ Award Number: KJCX20170205

The UHT of 120 and 135°C inactivated the microbial colonies and maintained the maintained the phenolic content by reducing the polyphenoloxidase activity. Moreover, the C9 aldehydes, especially the (E,Z)-­2,6-­nonadienal, presented the main aroma of the watermelon juice. The C9 aldehydes were formed as the results of the heat reduction and enzymatic metabolism. The temperature of 120 and 135°C reduced the alcohol dehydrogenase activity and well maintained the C9 aldehyde content of the watermelon juice. Hence, the temperature of 120°C of the UHT treatment was the optimal temperature for the production of the watermelon juice. KEYWORDS

(E,Z)-2,6-nonadienal, alcohol dehydrogenase, microbial colonies, polyphenoloxidase, ultrahigh temperature, watermelon

1 |  INTRODUCTION

sugarcane juice (Jittanit, Wiriyaputtipong, Charoenpornworanam, & Songsermpong, 2011). The temperature is the key factor of the UHT

Ultrahigh temperature (UHT) technique heats the feed at a high tem-

treatment. A higher temperature of the UHT treatment guarantees

perature in a short time, keeping the safety, and the nutrition of the

the safety of the juice (Charles-­Rodríguez et al., 2007). However, the

feed (Charles-­Rodríguez, Nevárez-­Moorillón, Zhang, & Ortega-­Rivas,

higher temperature of the UHT treatment leads to the degradation of

2007). At the beginning, the UHT technique was mainly used in the

the color, aroma, and nutritional quality of the juice (Tiwari, O’Donnell,

milk production, maintaining the safety, and extending the shelf life of

Muthukumarappan, & Cullen, 2009). For instants, the UHT treatment

the fresh milk. Currently, the UHT technique also inactivates the mi-

reduces the ascorbic acid content of the orange juice (Tiwari et al.,

crobial colonies of the watermelon juice (Zhang, Wang, Ma, Zhao, & Li,

2009), and the phenolics content of apricot nectars significantly

2015), orange juice (Walkling-­Ribeiro, Noci, Cronin, Lyng, & Morgan,

(Huang et al., 2013). Hence, it was important to find the optimal tem-

2009), cucumber juice (Liu, Zhang, Zhao, Wang, & Liao, 2016), and

perature to guarantee the safety of the juice as well as its qualities.

This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. © 2018 The Authors. Food Science & Nutrition published by Wiley Periodicals, Inc. Food Sci Nutr. 2018;1–8.

   www.foodscience-nutrition.com |  1

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WANG et al.

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Watermelon juice is sensitive to the heat, oxygen, light, ion, etc. (Aguiló-­Aguayo, Montero-­Calderón, Soliva-­Fortuny, & Martín-­ Belloso, 2010; Feng, Ghafoor, Seo, Yang, & Park, 2013; Liu, Wang, Zhang, et al., 2014; Zhang et al., 2011). In previous studies, our re-

a and a0 are the redness of a sample and the control, respectively; b and b0 are the yellowness of a sample and the control, respectively. The SSC was recorded by a pocket refractometer (Pal-­α, ATAGO, Japan) with distilled water as a blank.

sults proved that the UHT treatment was effective to inactivate the microbial colonies of the watermelon juice (Zhang et al., 2015). In this study, the temperature of the UHT treatment was further ex-

2.4 | Determination of phenolics content

plored to find the balance of the safety and qualities of the water-

The phenolic content was measured using Folin–Ciocalteu reagent

melon juice. Moreover, the key enzymes related to the formation of

(Yu, Perret, Harris, Wilson, & Haley, 2003). In brief, the reaction

the aroma were discussed to give a deeper insight into the qualities

mixture contained 50 μl of the sample, 250 μl of Folin–Ciocalteu

of the watermelon juice.

reagent, 0.75 ml of 20% sodium carbonate, and 3 ml of pure water. After the inoculation at 25°C for 2 hr, the absorbance at 765 nm was measured with the reaction mixture without sample as the control.

2 |  MATERIAL AND METHODS

The result is expressed as the gallic acid equivalent.

2.1 | Processing of the watermelon juice The mature watermelon (Citrullus lanatus var. Jingxin No.3) was purchased from a local fruit market. The fruits were round with regular stripes and weighted about 3–4 kg per fruit. The flesh of the fruits

2.5 | Measurement of polyphenoloxidase, alcohol dehydrogenase, and lipoxygenase activity The enzymatic extract was prepared by the watermelon juice followed

was red and crisp with a soluble solid content (SSC) of 11.5%–13.5%.

our recent methods (Zhang et al., 2011). Specifically, aliquot of 25 ml

The fruits were peeled and squeezed in a Philips juicer after stored

juice was stirred with 100 ml of the phosphate buffer (pH 6.0), 100 μl

at 4°C for 24 hr (HR1861, Philips Co. Beijing, China). The juice was

of Triton X-­100, and 3 g of polyvinylpyrrolidon. The mixture was

mixed with complex food additive including carboxymethylcellulose

magnetic stirred for 1 hr in the ice bath, and centigrade at 8,603 g

sodium (0.2%), ascorbic acid (0.025%), xanthan gum (0.05%), ethylene

for 15 min at 4°C. The supernatant was collected as the enzymatic

diamine tetraacetic acid (0.01%), carminum (0.005%), and sodium pyro-

extract for the following measurements, respectively.

phosphate (0.1%). The mixture was fully stirred, and was adjusted to the

PPO (polyphenol oxidase) activity was measured by a Shimadzu

pH 4.10 with the citric acid, and to the SSC of 8.0 with the high-­fructose

spectrophotometer (Ultraviolet-­1800, Shimadzu Corporation, Kyoto,

corn sirup (4502504-­01, Fresh Juice Industry [Kunshan] Co. Ltd.). And

Japan). Briefly, 100 μl of enzymatic extract was added to 1 ml sub-

then, the formulated juice was homogenized at the pressure of 50 MPa

strate (0.1 mol/L catechol in McIlvaine buffer, pH 5.0), and the in-

(NS101L2K, GEA Niro Soavi S.p.A., Parma, Italy), which was nominated

crease in absorbance at 400 nm at 25°C was recorded automatically

as the Unpasteurized. The Unpasteurized juice was pasteurized by UHT

for 30 min. One unit of PPO activity was defined as the change in ab-

treatment at the temperature of 110, 120, and 135°C for 2 s, which was

sorbance of 0.01/min at 420 nm, which was calculated from the linear

nominated as the UHT110, UHT120, and UHT135, respectively. The

part of the curve. The ADH (alcohol dehydrogenase) activity was estimated by a pho-

pasteurized juice was sterile filled in the 300 ml PET bottles.

tometric method with the p-­nitrosodimethylaniline as a substrate. The reaction mixture (2 ml) contained serum (0.1 ml), 1.8 ml of a 26 μmol/L

2.2 | Total microbial colonies

solution of substrate in 0.1 mol/L of sodium phosphate buffer, pH 8.5

The sample was serially diluted, plated in total count agar for total

and 0.1 ml of enzymatic extract containing 0.25 mol/L n-­butanol and

flora counts. The plates were incubated at 30°C for 48 hr, and the

5 mmol/L NAD. The reduction in p-­nitrosodimethylaniline was moni-

total microbial colonies were counted manually.

tored at 440 nm on a Shimadzu spectrophotometer (Ultraviolet-­1800, Shimadzu Corporation, Kyoto, Japan). The LOX (lipoxygenase) activity was determined by continu-

2.3 | Determination of color and SSC

ously monitoring the formation of conjugated dienes from linoleic

Color of the sample was measured in the reflectance mode for six

acid. The substrate consisted of 10 μl of linoleic acid, 4 ml of H2O,

times at 23°C (Chromameter CR-­300, Minolta, Japan). Color L*, a*,

1 ml of 0.12 N NaOH, and 5 ml of Tween 20. The enzymatic ex-

and b* value were measured and the total color difference (ΔE) was

tract was shaken and diluted up to 25 ml with pure water. The di-

calculated by Equation 1.

luted enzymatic extract of 100 μl was pipetted in a quartz with 2.7 ml of 0.2 mol/L phosphate buffer (pH 6.5) and 40 μl of the

ΔE = [(L − L0 )2 + (a − a0 )2 + (b − b0 )2 ]1∕2

(1)

substrate. The reaction started by adding the diluted enzymatic extract, and the absorbance was measured using a spectrophotometer (Ultraviolet-­1800, Shimadzu Corporation, Kyoto, Japan) at 234 nm

where ΔE is the total color difference between a sample and the con-

for 2 min at 22°C. A blank was prepared with 0.5 ml distilled water

trol, L and L0 are the lightness of a sample and the control, respectively;

and 3.0 ml substrate solution. The activity was determined from the

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WANG et al.

slope of the linear portion of the curve. One unit of LOX activity was

Volatile compounds were identified by comparison of their mass

defined as a change of 0.001 units of absorbance per minute and per

spectra and retention times with those of authentic standards, or by

milliliter of enzymatic extract.

comparison of Kovats’ retention indexes and mass spectrum, with those reported in the NIST Mass Spectral Search Program (version 2.0a) with