ARTICLE

The Relationship between Muscle Fiber Composition and Pork Taste-traits Assessed by Electronic Tongue System

Young-Hwa Hwang1http://orcid.org/0000-0003-3687-3535, Ishamri Ismail2http://orcid.org/0000-0003-4820-8292, Seon-Tea Joo1,2,*http://orcid.org/0000-0002-5483-2828
Author Information & Copyright
1Institute of Agriculture & Life Science, Gyeongsang National University, Jinju 52828, Korea
2Division of Applied Life Science (BK21+), Gyeongsang National University, Jinju 52828, Korea
*Corresponding author : Seon-Tea Joo; Division of Applied Life Science (BK21+), Gyeongsang National University, Jinju 52828, Korea Tel: +82-55-772-1943 Fax: +82-55-772-1949 E-mail: stjoo@gnu.ac.kr

© Copyright 2018 Korean Society for Food Science of Animal Resources. This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Received: Dec 04, 2018 ; Revised: Dec 14, 2018 ; Accepted: Dec 14, 2018

Published Online: Dec 31, 2018

Abstract

To investigate relationships of electronic taste-traits with muscle fiber type composition (FTC) and contents of nucleotides, porcine longissimus lumborum (LL), psoas major (PM), and infra spinam (IS) muscles were obtained from eight castrated LYD pigs. FTC and taste-traits in these three porcine muscles were measured by histochemical analysis and electronic tongue system, respectively. IS had significantly higher proportion of type I fibers while LL had significantly higher proportion of type IIB than other muscles (p<0.05). IS had the highest inosine monophosphate (IMP) content while LL had the lowest IMP content (p<0.05). In contrast, LL had significantly higher hypoxanthine content compared to PM and IS (both p<0.05). For taste-traits, IS had significantly higher umami and richness values but lower sourness value than LL and PM (p<0.05). Sourness and astringency values of LL were significantly higher than those of IS (p<0.05). The proportion of type IIB fiber was positively correlated with sourness and astringency but negatively correlated with saltiness. These results suggest that sourness and astringency tastes are increased with increasing proportions of type IIB fibers in porcine muscles due to increase of hypoxanthine content. These results also imply that umami and richness tastes are increased with increasing contents of type I and IIA fibers because of increased IMP content in porcine muscles.

Keywords: pork taste; electronic taste-traits; electronic tongue system; nucleotide compounds; fiber type composition

Introduction

Skeletal muscle consists of white and red muscle fibers whose ratio has a directly effect on meat quality. Red muscles with high myoglobin content mainly contain oxidative type I and oxidative/glycolytic type IIA fibers while white muscles contain glycolytic type IIB fibers with low myoglobin content (Morita et al., 1970). Fiber type compositions (FTCs) of skeletal muscles are affected by the location and function of the muscle within an animal. FTC in muscle is a major determinant factor of meat quality because contractile of myofibrils and metabolic properties of muscle are differentiated by types of muscle fiber (Joo et al., 2013). Previous studies have shown that these varying FTCs in porcine muscles are related to pork quality traits such as meat color, water-holding capacity, and tenderness (Choi and Kim, 2009; Jeong et al., 2017; Kim et al., 2013; Kim et al., 2018; Lee et al., 2012; Ryu and Kim, 2005; Ryu et al., 2008). However, few studies have reported the relationship between FTC in porcine muscles and pork taste-traits.

Taste plays an important role in sensory properties of meat together with other palatability traits such as flavor, texture, and juiciness. Meat has many taste-active substances such as free amino acids and adenosine 5’-triphosphate (ATP) metabolites. It is known that nucleotides and glutamic acid contribute to meat tastes, including delicious, umami, and brothy tastes (Nishimura, 1998, Nishimura et al, 1988). These components relative to umami have been considered influential contributors to the oro-sensory (sensory perception on taste) quality of meat (Fuke and Konosu, 1991). Especially, inosine monophosphate (IMP) in pork contributes to the preference of a human panel (Kawai et al., 2002; Okumura et al., 1996). IMP is released from pork muscle in the initial phase of moist heat cooking (Sasaki et al., 2007). According to Sasaki et al. (2005), the concentration of IMP in a pork water-extract varies among genetic species. Based on these findings, it is hypothesized that there are differences in content of nucleotides between porcine muscles because the rate of postmortem metabolism depends on the relative amount of muscle fiber types (Ryu and Kim, 2005; Hwang et al., 2010), resulting in different pork taste.

Many studies have used sensory evaluations to investigate meat quality and taste. However, the subjectivity and low reproducibility of sensory evaluations have often been criticized. For these reasons, an electronic tongue system has been developed to evaluate taste quality and intensity of many foods (Toko, 1996; Toko, 1998). It has been applied to meat and meat products (Chikuni et al., 2010; Okumura et al., 2004; Sasaki et al., 2007). Therefore, the objective of this study was to evaluate taste properties of three porcine muscles using an electronic tongue system in order to understand the relationship between FTC in porcine muscles and pork taste-traits.

Materials and Methods

Sample preparation

Three porcine muscles, longissimus lumborum (LL), psoas major (PM), and infra spinam (IS), were excised from carcasses of eight crossbred (Landrace×Yorkshire×Duroc), castrated male pigs. The average live weight of these pigs was 110.5±2.62 kg. Pigs were slaughtered by electrical stunning. Approximately 10±0.5 g of each muscle was taken and frozen in isopentane liquid nitrogen for histochemical analysis within 45 min postmortem. These samples were then stored at –80℃ until subsequent analyses. Meat quality were carried out after 36 h postmortem. For content of nucleotides and electronic taste-traits analysis, the analyses were performed after completing meat quality analysis. Three repetition were conducted and all measurements were made at 48 h postmortem.

Histochemical analyses

Serial transverse muscle sections with entire blocks (1.0×1.0×1.5 cm) mounted onto glass slides were cut into 10 μm thin slice using a cryostat microtom (HM525, Microm GmbH, Germany) at –20℃. The measurement of myosin adenosine triphosphatase (mATP) activities of the samples were based on Brooke and Kaiser (1970) after acid pre-incubation at pH 4.63. The stained sections was examined using an image analysis system (Image-Pro®plus 5.1, Media Cybernetics Inc., USA). The muscle fibers were differentiated into fiber type I, IIA, and IIB according to the nomenclature of Brooke and Kaiser (1970). Approximately 600 fibers per sample were counted and FTC was determined by fiber area percentages which was the ratio of total cross-sectional area of each fiber type to total fiber area measured.

Content of nucleotides

Meat sample (5 g) was homogenized in a 50 mL conical tube with 20 mL of 0.5 M perchloric acid in the ice bath for 1 min based on the modified method of Yang et al. (2002). The extraction mixture was centrifuged at 3,000×g for 15 min at 4℃. Supernatant was filtered with Whatman filter paper No. 1. The residuum was mixed with 10 mL of 0.5 M perchloric acid. The mixture was again homogenized and filtered. The filtrate was neutralized to pH 6 with 5 M potassium hydroxide. The neutralized filtrate was centrifuged (3,000×g at 4℃ for 10 min) and filtered with Whatman No. 4. The filtered supernatant was added with 0.5 M perchloric acid (pH 6.0) to reach final volume of 50 mL. The solution was filtered again through a 0.45 μm filter and stored at –25℃ prior to analysis. Analysis of nucleotides was performed using an Agilent 1100 HPLC system with Eclipse Plus C18 column (4.6×100 mm, 3.5 μm). Mobile phase A consisted of 0.06 M K2HPO4 and 0.04 M KH2PO4 adjusted to pH 7.0. Mobile B consisted 80% methanol and 20% Mili-Q water. Peaks were detected and analyzed at 254 nm with a diode array detector (DAD). HPLC separation was achieved using continuous gradient elution between Phase A and Phase B. The elution program of Phase B was: 0 min (0%), 10 min (0%), 11 min (100%), and 12 min (0%). The program then took 4 min to return to initial conditions and stabilize. Flow rate of the mobile phase was set at 1.2 mL/min with 20 μL injection volume. Total retention time was about 5 min and the gradient was run for 16 min to ensure full separation. All ATP, ADP, AMP, IMP, inosine, and hypoxanthine in samples were identified by comparison with retention time of standards.

Meat quality traits

Color measurements of different porcine muscles were performed using a colorimeter (Minolta CR -300, Minolta Co., Japan) that was standardized with a white plate (Y=93.5, X=0.3132, y=0.3198) before measuring. Color parameters were expressed as L* (lightness), a* (redness), b* (yellowness), polar-coordinate Chroma (C*), and hue angle (h°).

Water-holding capacity (WHC) of all samples was evaluated by released water (RW) % and cooking loss (CL) %. CL % was determined as described by Hwang et al. (2010) by weight different before and after cooking. RW % was based on method of Joo (2018). Approximately 3.0 g of meat sample was placed on a filter-paper between two thin plastic films. A load of 2.5 kg was then applied for 5 min. After accurately removing the compressed meat sample, the damp filter-paper and two plastic films were rapidly weighed. The percentage of RW % was calculated as follows: RW %=[(damp filter-paper and plastic films weight)–(filter-paper and plastic films weight)/meat sample weight]×100.

Warner–Bratzler shear force (WBSF) values were measured using an Instron Universal testing Machine (Model 4400, Instron Co., USA) with a V shaped shear blade. Samples (1.0 cm–diameter cores obtained from muscle) were cooked to have an internal temperature of 70℃ for 30 min. Peak force was obtained using 100 N load cell tension applied at a crosshead speed of 250 mm/min. The full-scale load was 50 kg.

Electronic tongue measurements

An electronic tongue system (INSENT SA402B electric taste sensing system, INSENT, Tokyo, Japan) was used to determine pork taste-traits. This system is composed of five taste sensors of polymer membranes fixing different lipids. These sensors, CA0, C00, AE1, AAE, and CT0, are designed to respond to individual tastes of sourness, bitterness, astringency, umami, and saltiness, respectively (Toko, 1996; Toko, 1998). Fresh 30 mM KCl solution containing 0.3 mM tartaric acid (corresponding to saliva) was used as the reference solution (RS). It was also used to rinse electrodes after every measurement. Vr (membrane potential in reference solution) is the potential when the electrode is dipped into the RS for the first time and Vs (membrane potential in sample solution) is another potential for the sample solution or suspension. Vr’ (new membrane potential in reference solution) is the new potential of the RS when the electrode is dipped into the RS again. CPA (change of membrane potential caused by adsorption) is the difference (Vr’–Vr) between potentials of the RS before and after sample measurement. It represents aftertaste. Each measuring time was set at 30 sec. Electrodes were rinsed after each measurement.

Each porcine muscle sample was measured after electric potentials of all membranes had been stabilized in standard pork taste (SPT) solution. A synthetic solution containing 0.02% lactic acid (sourness), 0.4% monosodium glutamate (umami), 0.001% quinine hydrochloride (bitterness), 0.05% sodium chloride (saltiness), and 0.8% sucrose (sweetness) was used as SPT solution. Sample solutions were prepared by extracting ground porcine muscles (100 g) with 400 mL hot water (1:4, w/v) of 95℃ for 10 min followed by centrifugation at 3,000×g for 10 min before analysis. All measurements were made at room temperature of 28℃.

Statistical analysis

All experimental data were analyzed by analysis of variance (ANOVA) procedure of statistical analysis systems (SAS, 2002). Duncan's multiple range test was used to determine significant differences among means at 5% level of significance (SAS, 2002). Pearson correlation coefficients were used to determine the relationship between FTC and taste-traits of electronic tongue system using partial correlation coefficients (SAS, 2002).

Results and Discussion

A clear difference in FTC was observed among three porcine muscles (Table 1). IS muscle had significantly higher proportion of type I fibers than LL and PM muscles (p<0.05). There was no significant difference in the proportion of type I fibers between PM and IS muscles. The proportion of type IIA fibers was significantly lower in LL muscle than that in other muscles (p<0.05). The proportion of type IIA was not significantly different between PM and IS muscles. There were significantly differences in the proportion of type IIB fibers among LL, PM, and IS muscles. LL muscle had the highest proportion of type IIB fibers while IS muscle showed the lowest proportion of type IIB fibers among three porcine muscles.

Table 1. Differences in fiber type composition among three porcine muscles
Porcine muscles Fiber type composition (%)
Type I Type IIA Type IIB
M. longissimus lumborum 5.76±0.78C 4.76±1.00B 89.48±0.93A
M. psoas major 9.63±1.61B 20.46±2.10A 69.91±3.28B
M. infra spinam 51.06±2.86A 20.24±2.74A 28.70±2.20C

All values are presented as means±SE (n=8).

Different superscripts in the same column (A–C) indicate significant difference (p<0.05).

Download Excel Table

Joo et al. (2013) have indicated that histochemical characteristics of muscle fiber depend on muscle location and function in animals. The higher proportion of type IIB fibers in LL muscle was similar to results of Kim et al. (2013) and Realini et al. (2013). The higher proportion of type I fibers in IS muscle was expected because deep muscles involved in maintaining posture are more oxidative and containing more type I fibers than more superficial muscles involved in rapid movements (Joo et al., 2013). Since this FTC variation between muscles is directly related to metabolic and contractile properties, there could be considerable variations in pork quality characteristics and taste-traits between various porcine muscles within a carcass.

As expected, significant differences in pork quality traits were observed among three porcine muscles (Table 2). LL muscle had significantly higher L* values while IS and PM muscles had significantly higher a* and b* values compared to other muscles (p<0.05). RW % was significantly higher in LL muscle than that in PM and IS muscles (p<0.05), although there was no significant difference in cooking loss % among the three muscles. There were significant differences in WBSF values among three muscles (p<0.05), with IS having the highest WBSF value, followed by LL and PM muscle.

Table 2. Differences in meat quality measurements among three porcine muscles
Variables Muscles
LL PM IS
Meat color CIE L* 49.52±0.78A 45.14±1.02B 44.11±0.59B
                 CIE a* 6.72±0.41B 14.39±0.55A 13.97±0.66A
                 CIE b* 1.11±0.23B 2.57±0.41A 3.08±0.30A
Released water (%) 10.47±1.30A 7.00±0.95B 5.85±0.93B
Cooking loss (%) 22.28±2.20 20.72±2.10 20.21±1.83
WBSF (kg/cm2) 4.08±0.21B 3.55±0.11C 5.01±0.16A

All values are presented as means±SE (n=8).

Different superscripts in the same row (A–C) indicate significant difference (p<0.05).

LL, M. longissimus lumborum; PM, M. psoas major; IS, M. infra spinam; WBSF, Warner-Bratzler shear force.

Download Excel Table

A few studies have been conducted to compare pork quality traits between porcine muscles in relation to FTC (Kim et al., 2018; Realini et al., 2013; Ruusunen and Puolanne, 2004). Most of these studies involving pork quality traits and FTC have been done mainly using the longissimus dorsi muscle. It is well known that variation in pork quality is related to heterogeneity in glycogen depletion between different muscle fiber types (Klont et al., 1998). Generally, glycolysis and onset of rigor mortis are faster in white muscles than those in red muscles. Therefore, the higher L* value in LL muscle is expected because it has a high glycolytic capacity (Joo et al., 2013; Kim et al., 2013). The higher a* value in IS and PM muscles in this study was similar to results of Realini et al. (2013), reporting that muscle redness was positively correlated with type I fiber but negatively associated with type II fiber. It is certain that the higher RW % in LL muscle is due to higher proportion of type IIB fibers because an increase in the proportion of large IIB fibers causes poor water-holding capacity of pork (Kim et al., 2013). Also, the higher WBSF value in IS muscle is probably due to higher proportion of type I fibers. Fiber type I has a positive correlation with shear force values in contrast fiber type IIB has a negative correlation to meat tenderness (Kim et al., 2013; Ryu and Kim, 2005).

Contents of nucleotide compounds in three porcine muscles are shown in Fig. 1. IMP showed the highest content (148–447 mg/100 g), followed by inosine (28–39 mg/100 g), hypoxanthine (7.1–18.6 mg/100 g), ADP (5.7–8.0 mg/100 g), AMP (2.0–2.6 mg/100 g), and ATP (1.1–2.2 mg/100 g) in porcine muscles at 48 h postmortem. There were significantly differences in contents of all nucleotide compounds among three muscles (p<0.05). IS muscle had the highest IMP content while LL muscle had the lowest IMP content (p<0.05). In contrast, LL muscle had significantly higher hypoxanthine content than PM and IS muscles (p<0.05). IS muscle had significantly higher ATP and ADP contents but lower inosine content than LL and PM muscles (p<0.05).

kosfa-38-6-1305-g1
Fig. 1. Contents of nucleotide compounds (mg/100 g muscle) in porcine M. longissimus lumborum (LL), M. psoas major (PM), and M. infra spinam (IS) at 48 h postmortem; Different letters in bars among muscle samples indicate significant differences (p<0.05).
Download Original Figure

Many studies have shown that IMP contributes to meat taste properties such as delicious, umami, and brothy tastes (Fuke and Konosu, 1991; Kawai et al., 2002; Nishimura et al., 1988; Shi et al., 2017). The IMP content relative to umami has been considered an important contributor to the oro-sensory quality of meat (Fuke and Konosu, 1991). Okumura et al. (1996) have reported that IMP in pork can positively influence the panelist preference. According to Sasaki et al. (2007), IMP is released from the pork muscle during the initial phase of moist heat cooking. The concentration of IMP in a water-extract of pork muscle is different among genetic pig species (Sasaki et al., 2005). In the present study, it was clearly shown that the concentration of IMP was significantly different among three porcine muscles which had different FTCs. These three porcine muscles also had different concentrations of hypoxanthine related to bitter taste (Ozogul et al., 2010). Therefore, it is easily expected that taste-traits are also different among these three muscles due to different concentrations of nucleotides. In this regard, our previous studies have shown differences in sensory evaluation scores among various bovine muscles with different FTCs (Hwang et al., 2010; Jung et al., 2015; Jung et al., 2016).

Sensory evaluation results of three porcine muscles using the electronic tongue system are presented in Fig. 2. When relative taste-traits intensity values were computed from the SPT solution, all three porcine muscles showed negative values for sourness, astringency, and saltiness but positive values for umami, richness, and bitterness. All taste-traits intensity values except bitterness were significantly different among the three muscles (p<0.05). IS muscle had significantly higher umami and richness values but lower sourness value than LL and PM muscles (p<0.05). Sourness and astringency values of LL muscle were significantly higher than those of IS muscle (p<0.05). There were no significant differences in umami, sourness, or astringency values between LL and PM muscles. The saltiness values of LL muscle was significantly lower than that of IS or PM muscle (p<0.05).

kosfa-38-6-1305-g2
Fig. 2. Relative changes in taste-traits of three porcine muscles from baseline in SPT solution. LL, M. longissimus lumborum; PM, M. psoas major; IS, M. infra spinam; SPT, standard pork taste. Different letters in bars indicate significant differences (p<0.05) of taste-traits among muscles within the box.
Download Original Figure

The higher umami value in IS muscle was expected because IS muscle showed the highest IMP content (Fig. 1). In contrast, umami value of LL muscle was lower than that of IS muscle due to the lowest IMP content in LL muscle. These results confirmed results of others showing that IMP content was related to umami taste of meat (Fuke and Konosu, 1991; Nishimura et al., 1989). Our data also showed that IS muscle had higher richness value reflecting persistent intensity of umami taste. The strong umami intensity in IS muscle is probably due to its higher proportion of type I fibers. In contrast, higher sourness and astringency values in LL muscle are due to its higher proportion of type IIA fibers. According to Chikuni et al. (2010), muscle fiber types are strongly related to differences in sour taste, with fast-type muscle having significantly lower pH due to its higher lactic acid content than slow-type muscle. In the present study, FTC in muscle not only affected sour taste, but also astringency taste.

Correlations of electronic taste-traits with FTC and nucleotide compounds are presented in Table 3. These results showed that contents of type I and type IIB fibers were inversely correlated to electronic taste-traits. The proportion of type IIB fiber was positively correlated with sourness and astringency but negatively correlated with saltiness. Interestingly, similar tendencies were found between hypoxanthine content and taste-traits. In contrast, the proportion of type I fiber was positively correlated with umami, richness, and saltiness but negatively correlated with sourness and astringency. IMP content showed correlation tendencies with electronic taste-traits similar to the proportion of type I fiber. These correlations clearly showed that sourness and astringency tastes were increased with increasing content of type IIB fibers in porcine muscles due to increase of hypoxanthine content. These results suggest that umami and richness tastes are increased with increasing content of type I and IIA fibers because of increased IMP content in porcine muscles.

Table 3. Correlation coefficients (r) of electronic taste-traits with fiber type composition and contents of nucleotides in porcine muscles
Sourness Bitterness Astringency Umami Richness Saltiness
Muscle fiber
    Type I –0.58** 0.16 –0.48* 0.59** 0.87*** 0.61**
    Type IIA –0.35 0.11 –0.30 0.46** 0.51** 0.68***
    Type IIB 0.57** –0.17 0.48* –0.62** –0.85*** –0.69***
Nucleotides
    ATP –0.67*** –0.38 –0.42* 0.69*** 0.60** 0.26
    ADP –0.19 0.18 –0.21 0.20 0.59** 0.27
    AMP –0.05 –0.23 0.21 –0.03 –0.02 –0.33
    IMP –0.50* 0.13 –0.44* 0.54** 0.74*** 0.69***
    Inosine 0.24 –0.12 0.47* –0.35 –0.54** –0.30
    Hypoxanthine 0.54** –0.06 0.41* –0.55** –0.69*** –0.63**

* p<0.05

** p<0.01

*** p<0.001.

Download Excel Table

Conclusions

The different composition of muscle fiber types were clearly observed among three porcine muscles. These differences affected content of nucleotide compounds and electronic taste-traits. Pork sourness and astringency tastes were increased with increasing content of type IIB fibers in porcine muscles due to increase of hypoxanthine content. Pork umami and richness tastes were also increased with increasing contents of type I and IIA fibers due to increase of IMP content in porcine muscles.

Acknowledgements

This research was supported by the Korean Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry and Fisheries (IPET) through the Agri-Bioindustry Technology Development Program, funded by Ministry of Agriculture, Food and Rural Affairs (MAFRA) (Project No. 118052-03), Korea.

Notes

Conflicts of Interest

The authors declare no potential conflict of interest.

References

1.

Brooke MH, Kaiser KK. Muscle fiber types: How many and what kind?. Arch Neurol. 1970; 23:369-379

2.

Chikuni K, Oe M, Sasaki K, Shibata M, Nakajima I, Ojima K, Muroya S. Effects of muscle type on beef taste-traits assessed by an electric sensing system. Anim Sci J. 2010; 81:600-605

3.

Choi YM, Kim BC. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livest Sci. 2009; 122:105-118

4.

Fuke S, Konosu S. Taste-active components in some foods: A review of Japanese research. Physiol Behav. 1991; 49:863-868

5.

Hwang YH, Kim GD, Jeong JY, Hur SJ, Joo ST. The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers. Meat Sci. 2010; 86:456-461

6.

Jeong JY, Jeong TC, Yang HS, Kim GD. Multivariate analysis of muscle fiber characteristics, intramuscular fat content and fatty acid composition in porcine longissimus thoracis muscle. Livest Sci. 2017; 202:13-20

7.

Joo ST, Kim GD, Hwang YH, Ryu YC. Control of fresh meat quality through manipulation of muscle fiber characteristics. Meat Sci. 2013; 95:828-836

8.

Jung EY, Hwang YH, Joo ST. Chemical components and meat quality traits related to palatability of ten primal cuts from Hanwoo carcasses. Korean J Food Sci An. 2015; 35:859-866

9.

Jung EY, Hwang YH, Joo ST. The relationship between chemical compositions, meat quality, and palatability of the 10 primal cuts from Hanwoo steers. Korean J Food Sci An. 2016; 36:145-151

10.

Kawai M, Okiyama A, Ueda Y. Taste enhancements between various amino acids and IMP. Chem Senses. 2002; 27:739-745

11.

Kim GD, Jeong JY, Jung EY, Yang HS, Lim HT, Joo ST. The influence of fiber size distribution of type IIB on carcass traits and meat quality in pigs. Meat Sci. 2013; 94:267-273

12.

Kim GD, Yang HS, Jeong JY. Intramuscular variations of proteome and muscle fiber type distribution in semimembranosus and semitendinosus muscles associated with pork quality. Food Chem. 2018; 244:143-152

13.

Klont RE, Brocks L, Eikelenboom G. Muscle fibre type and meat quality. Meat Sci. 1998; 49:S219-S229

14.

Lee SH, Choe JH, Choi YM, Jung KC, Rhee MS, Hong KC, Lee SK, Ryu YC, Kim BC. The influence of pork quality traits and muscle fiber characteristics on the eating quality of pork from various breeds. Meat Sci. 2012; 90:284-291

15.

Morita S, Cassens RG, Briskey EJ, Kauffman RG, Kastenschmidt LL. Localization of myoglobin in pig muscle. J Food Sci. 1970; 35:111-112

16.

Nishimura T, Rhue MR, Okitani A, Kato H. Components contributing to the improvement of meat taste during storage. Agric Biol Chem Tokyo. 1988; 52:2323-2330

17.

Nishimura T. Mechanism involved in the improvement of meat taste during postmortem aging. Food Sci Technol Int. 1998; 4:241-249

18.

Okumura T, Inuzuka Y, Nishimura T, Arai S. Changes in sensory, physical and chemical properties of vacuum packed pork loins during the prolonged conditioning at 4℃. J Anim Sci Technol. 1996; 67:360-367.

19.

Okumura T, Yamada R, Nishimura T. Sourness-suppressing peptides in cooked pork loins. Biosci Biotechnol Biochem. 2004; 68:1657-1662

20.

Ozogul F, Ozden O, Ozogul Y, Erkan N. The effects of gamma-irradiation on the nucleotide degradation compounds in sea bass (Dicentrarchus labrax) stored in ice. Food Chem. 2010; 122:789-794

21.

Realini CE, Venien A, Gou P, Gatellier P, Perez-juan M, Danon J, Astruc T. Characterization of Longissimus thoracis, Semitendinosus and Masseter muscles and relationships with technological quality in pigs. 1. Microscopic analysis of muscles. Meat Sci. 2013; 94:408-416

22.

Ruusunen M, Puolanne E. Histochemical properties of fibre types in muscles of wild and domestic pigs and the effect of growth rate on muscle fibre properties. Meat Sci. 2004; 67:533-539

23.

Ryu YC, Choi YM, Lee SH, Shin HG, Choe JH, Kim JM, Hong KC, Kim BC. Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Sci. 2008; 80:363-369

24.

Ryu YC, Kim BC. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci. 2005; 71:351-357

25.

Sasaki K, Motoyama M, Mitsumoto M. Changes in the amounts of water-soluble umami-related substances in porcine longissimus and biceps femoris muscles during moist heat cooking. Meat Sci. 2007; 77:167-172

26.

Sasaki K, Tani F, Sato K, Ikezaki H, Taniguchi A, Emori T, Iwaki F, Chikuni K, Mitsumoto M. Analysis of pork extracts by taste sensing system and the relationship between umami substances and sensor output. Sens Mater. 2005; 17:397-404.

27.

Shi C, Cui J, Liu X, Zhang Y, Qin N, Luo Y. Application of artificial neural network to predict the change of inosine monophosphate for lightly salted silver carp (Hypophthalmichthys molitrix) during thermal treatment and storage. J Food Process Preserv. 2017; 41:e13246

28.

Toko K. Taste sensor with global selectivity. Mater Sci Eng C. 1996; 4:69-82

29.

Toko K. Electronic tongue. Biosens Bioelectron. 1998; 13:701-709

30.

Yang NC, Ho WM, Chen YH, Hu ML. A convenient one-step extraction of cellular ATP using boiling water for the luciferin-luciferase assay of ATP. Anal Biochem. 2002; 306:323-327

Journal Title Change

We announce that the title of our journal and related information were changed as below from January, 2019.

 

Before (~2018.12)

After (2019.01~)

Journal Title

Korean Journal for Food Science of Animal Resources

Food Science of Animal Resources

Journal Abbreviation

Korean J. Food Sci. An.

Food Sci. Anim. Resour.

eISSN

2234-246X

2636-0780

pISSN

1225-8563

2636-0772

Journal Homepage

http://www.kosfaj.org

Same

JCR Citation Indexing

SCIE

SCIE

I don't want to open this window for a day.