Effect of Whey Protein Concentrate on GelForming Ability of Rohu (Labeo rohita)

Transcription

1 Journal of Advaned Agriultural Tehnologies Vol. 4, No. 3, September 2017 Effet of Whey Protein Conentrate on GelForming Ability of Rohu (Labeo rohita) Phatthira Sutloet and Warangkana Sompongse Department of Food Siene and Tehnology, Faulty of Siene and Tehnology, Thammasat University, Pathum Thani, Thailand Katsuji Morioka Laboratory of Aquati Produt Utilization, Faulty of Agriulture, Kohi University, Monobe 200, Nankoku, Kohi , Japan enzyme has an adverse effet on the gel-forming, produing too soft and mushy a gel. Ref. [3], [4] reported that the endogenous protease is ativated at 50-70oC. This phenomenon is known as modori, and auses destrution of the three-dimensional struture of the gel network [5], [6]. To overome the softening of modori gel, a variety of food grade inhibitors have been used to inhibit the degradation of the myofibrillar protein, inluding beef plasma protein (BPP), egg protein, and whey protein onentrate (WPC) [7], [8], [5], [9]. From researh, BPP ontains α2 maroglobulin (α2m) and kininogens that inhibit the endogenous protease ativity [10]. Egg protein ontains ovomuoid, whih inhibits trypsin, and ovoinhibitors, whih inhibit trypsin and hymotrypsin. However, BPP was prohibited beause of the ourrene of mad ow disease and egg white has an undesirable egg-like odour and is expensive [7]. However, the addition of WPC an inhibit endogenous protease resulting from the protein that has a moleular weight of 100,000 Da. It an inhibit papain (ysteine protease) and trypsin (serine protease) [10]. In addition, WPC is generally reognized as safe (GRAS) by the U.S Food and Drug Administration [11] and had no adverse effet on the attributes of the gel [12], [5]. Whey protein onentrate (WPC) is obtained from heese manufaturing and is ommonly used as a thikener, whipping agent, emulsifier, whitener, or gelling agent [13]. Moreover, WPC has been used in various foods suh as sausage, meat balls and low-salt fish produts [14], [12], [5]. Furthermore, researh has reported that the addition of WPC improved the gel strength in Paifi whiting, Alaska pollok [15], [12], bigeye snapper (Priaanthus tayenus), goatfish (Mulloidihthys vaniolensis), threadfin bream (Nemipterus bleekeri), and lizardfish (Saurida tumbil) [5]. Nevertheless, no study has reported on the addition of WPC to the gel from rohu. Consequently, the objetive of this study was to investigate the effet of whey protein onentrate on the gel-forming ability of rohu (Labeo rohita). Abstrat The gel-forming ability of rohu (Labeo rohita) was investigated. Unwashed and washed gel was prepared under different setting onditions inluding kamaboko gel (40oC, 30 min) and modori gel (60 and 65oC for washed and unwashed gel, respetively, 30 min), then both gels were heated at 90oC for 20 min. The gel-forming ability was investigated using the folding test, gel strength, and waterholding apaity expressed by the expressible water ontent. The addition of whey protein onentrate (WPC) at 3% improved the folding test, gel strength, and water-holding apaity of unwashed modori gel. The addition of (WPC) at 2% inreased the gel strength of unwashed kamaboko gel and improved the water-holding apaity. The inreases in gel strength of both washed gels were found with WPC at 1%. The water-holding apaity of washed modori gel was improved at this onentration, while the addition of WPC did not affet the water-holding apaity of the washed kamaboko gel. Although WPC improved the modori gel, the inreases were not as high as those for the kamaboko gel either unwashed or washed. Determinations of whiteness showed that the addition of WPC affeted the whiteness of unwashed gel, while not affeting the washed gel. Index Terms rohu (Labeo rohita), gel-forming ability, modori gel, kamaboko gel, whey protein onentrate I. INTRODUCTION Rohu (Labeo rohita) is a freshwater fish speies that is widely-used in aquaulture in Thailand. Based on the data for the year 2010, the amount of rohu produed in Thailand was 1167 tons, with a market value of 42 million Baht [1]. Nevertheless, the market value of rohu is onsidered low. Furthermore, rohu have small pin bones in their flesh, whih hinders their utilization for ooking [2]. This might be the reason that rohu is less utilized than other fish. To expand utilization and the market value of rohu, the flesh ould be proessed by mining or for use as surimi. The degradation of myofibrillar protein by endogenous protease has been widely studied. The presene of this Manusript reeived November 25, 2016; revised May 26, Journal of Advaned Agriultural Tehnologies doi: /joaat

2 Journal of Advaned Agriultural Tehnologies Vol. 4, No. 3, September 2017 II. MATERIALS AND METHODS A. Materials Rohu (Labeo rohita) was purhased from Klong Si Fish Market (Pathum Thani, Thailand). Fish were paked in an ie box and immediately transported to the laboratory. Whey protein onentrate (WPC) was obtained from Open Country Dairy Ltd. (Wahora, New Zealand) B. Preparation of Washed and Unwashed Mines The fish were gutted and washed with tap water. The fillet was mined using a meat grinder (2 mm hole diameter; AT950A, Kenwood, England). The mined fish was divided into two groups, unwashed and washed. For preparation of the washed mine, ied water was added at a ratio of 4:1 (w/w), then the mixture was stirred for 5 min and left to stand without stirring for 5 min. After that, the mixture was filtered through heeseloth. The washing proess was repeated three times, twie with ied water and the third time with old 0.3% (w/v) sodium hloride solution. C. Preparation of Washed and Unwashed Gels To prepare the gels, 2.5% salt was added to all the samples. WPC was added at onentrations of 1%, 2% and 3% with an untreated sample kept as a ontrol. The moisture ontent was adjusted to 85% by the addition of ied water during the grinding of the mixture. Then, the batter was stuffed into ellulose asing (2.5 m diameter) and tightly sealed at both ends. The temperature of the batter was maintained below 12 o C throughout the proess. The batter was divided into two groups aording to the type of gel: kamaboko (K) and modori (M) gel. The kamaboko gel was heated at 40 o C for 30 min followed by heating at 90 o C for 20 min. The modori gel was heated at 60 o C (washed gel) and 65 o C (unwashed gel) for 30 min and then heated at 90 o C for 20 min. After heating, all gels were immediately ooled in ied water until the ore temperature of the samples fell below 10 o C. The samples were stored overnight at 4 2 o C prior to further analysis. D. Determination of Folding Test The gel samples (5 mm thikness, 2.5 m diameter) were folded into halves and quarters. The proedure for the folding test followed [16]. E. Determination of Textural Properties The textural properties of the gel samples (breaking fore (g) and deformation (m)) were determined using a texture analyzer (TA -XTPlus, Stable Miro Systems, Surrey, UK) with a spherial probe (5 mm diameter; 60 mm min -1 test speed). Gel samples were allowed to reah room temperature ( 30 C). Five ylinder-shaped samples 2.5 m in length were prepared from eah gel. The gel strength (g.m) was expressed as the breaking fore multiplied by breaking distane. F. Determination of Expressible Water The expressible water ontent was measured aording to the method of [17] with slightly modifiation. Gel samples were ut into piees of 0.5 x 1 x 0.5 m 3, weighed (X) and plaed between Whatman paper (No.1), with three piees of paper at the bottom and two piees on the top. A standard weight (5 kg) was plaed on the gel samples for 2 min and then removed. The samples were weighed again (Y). Expressible water was alulated using the following equation and expressed as perentage of sample weight: Expressibl e water (%) [( X Y) /( X ) 100 (1) G. Determination of Whiteness The whiteness of the gel samples (2.5 m thikness, 2.5 m diameter) were determined using a olorimeter (HunterLab, ColorFlex CX2687, USA). D65 illuminant was used as the light soure. CIE L*, a*, and b* values were measured. Whiteness was alulated using the following equation [18]: / 2 Whiteness 100 [(100 L*) a* b* ] (2) H. Statistial Analysis The experiment was designed using a ompletely randomized design. Data were subjeted to analysis of variane. A Dunan s new multiple range test was used to determine the differenes between sample means at P<0.05. All experiments were done in tripliate. III. RESULTS AND DISCUSSION A. Effet of Whey Protein Conentrate on Textural Properties of Unwashed Rohu Gel Folding test and gel strength of kamaboko (K) and modori (M) gel of unwashed rohu gel ontaining WPC at different levels (0-3%) are shown in Fig. 1. The onentration signifiantly affeted the folding test and gel strength of modori and kamaboko gels (P<0.05). For modori gel, the folding test inreased as the onentration inreased. The inrease was signifiantly greater with the addition of WPC at 2-3%, ompared to that of the ontrol (P<0.05). The gel strength of the modori gel inreased as the onentration inreased, but not signifiantly (P>0.05). No signifiant differene in the folding test of kamaboko gel was observed (P>0.05). The strength of the kamaboko gel inreased as the onentration inreased. The gel strength of gels with WPC above 2% was higher than that of the ontrol. These results agreed with the findings in [7] that the addition of WPC improved the textural attributes of Paifi whiting surimi heat set gels. This may be beause the addition of 3% WPC to the unwashed Paifi whiting mine redued the relative enzyme ativity by about 80% [7]. The harateristis of kamaboko and modori gel were investigated. As shown in Fig. 1, the kamaboko gel had a higher folding test and gel strength than the modori gel. The inreased textural properties of gel set at 40 o C (kamaboko gel) may be due to endogenous transglutaminase (TGase). TGase atalyses the ayl transfer reation between glutamine and lysine residues of musle proteins, resulting in the formation of - ( - glutamyl) lysine ross-links [19], [20]. In addition, setting 2017 Journal of Advaned Agriultural Tehnologies 227

3 Journal of Advaned Agriultural Tehnologies Vol. 4, No. 3, September 2017 gel at 65 o C (modori gel) ould be affeted by endogenous protease. Previous studies [3], [4] have reported that the weakening of gel is aused by endogenous protease under heating at o C. Moreover, these enzymes degrade the myofibrillar protein, espeially myosin, and prevent the development of the three-dimensional gel network, reduing the quality of the gel [21], [22], [19]. The modori gel improved with the addition of 3% WPC, though the textural properties were not as high as those of kamaboko gel. This finding implied that the addition of WPC at 3% and 2% ould improve the textural properties of modori gel and kamaboko gel, respetively. as the onentration inreased, no marked derease was found with the addition of further WPC. The results showed that the modori gel had a higher expressible water ontent than the kamaboko gel. This inrease indiated the poor water-holding apaity of gel [5]. This result suggested that the modori gel network was poor in water-holding apaity ompared with the kamaboko gel, whih might be due to the role of endogenous protease that is ativated under heating at o C [3], [4]. Nevertheless, the addition of 1% and 3% WPC improved the water-holding apaity of kamaboko and modori gels (P>0.05), respetively, ompared with that of the ontrol. This result might be due to the protein additives reduing the moisture ontent and inreasing the density of the surrounding protein matrix, as its high water-holding apaity, auses swell and inreases elastiity. [23]. This result oinided with those from the textural properties. WPC improved the modori gel ontaining at 3%, but the water-holding apaity was not as high as that of kamaboko gel. This finding suggested that the addition of WPC at 3% and 1% ould improve the water holding apaity of modori and kamaboko gel, respetively. Expressible water (%) d e e e ab a b Conentration of WPC (%) Figure 2. Expressible water of unwashed rohu gels ontaining whey protein onentrate at various onentrations. standard deviation from three times determination. Different letters on eah bar indiate signifiant differenes (P<0.05). Figure 1. Folding test (A) and gel strength (B) of unwashed rohu gels ontaining whey protein onentrate at various onentrations. standard deviation from five times determination. Different letters on eah bar indiate signifiant differenes (P<0.05). B. Effet of Whey Protein Conentrate on Expressible Water of Unwashed Rohu Gel The expressible water ontent of unwashed kamaboko (K) and modori (M) rohu gel at different levels of WPC (0-3%) is shown in Fig. 2. For both of the gels, the expressible water ontent dereased as the onentration inreased. For modori gel, the lowest expressible water ontent was obtained in gel with 3% WPC. Although the expressible water ontent of the kamaboko gel dereased C. Effet of Whey Protein Conentrate on Whiteness of Unwashed Rohu Gel The whiteness of unwashed kamaboko (K) and modori (M) gel of rohu at different levels of WPC (0-3%) are shown in Fig. 3. For both gels, the whiteness inreased as the onentration inreased. For modori gel, no marked inrease was found in gels with the addition of further WPC. The highest whiteness of kamaboko gel was found with 3%WPC. From the results, the addition of 3% and 1% WPC inreased the whiteness of kamaboko and modori gel (P>0.05), respetively, ompared to that of ontrol gel. These results revealed that gel samples might be affeted by the light ream olor of WPC. However, the result was not in agreement with [5], whih reported that the whiteness of kamaboko gel of bigeye snapper and goatfish dereased with the addition of 3% WPC. The 2017 Journal of Advaned Agriultural Tehnologies 228

4 Journal of Advaned Agriultural Tehnologies Vol. 4, No. 3, September 2017 olor of the WPC might affet the olor of gels in different ways, depending on the native olor of the mine. Whiteness b b ab b a a a appeared ineffetive in removing the endogenous protease. This agreed with the findings of [25] that the protease level of lizardfish (Saurida undosquamis) musle remained at 70% after washing. Ref. [26] suggested that the strength of maeso lizardfish (Saurida undosquamis) gel heated at o C was not improved by washing. Ref. [12] reported that Paifi whiting surimi gel set without inhibitors at 60 o C for 30 min followed by 90 o C, was too soft for textural measurement owing to the role of the proteinase. In addition, [6] reported that lizardfish surimi gel set at 65 o C without inhibitors ould not form a strong gel due to myosin heavy hain (MHC) loss. Although the modori gel was improved by WPC at 3%, the gel strength was not as high as that of kamaboko gel. This suggested that the addition of WPC at 1% ould improve the textural properties of modori and kamaboko gel. Conentration of WPC (%) Figure 3. Whiteness of unwashed rohu gels ontaining whey protein onentrate at various onentrations. standard deviation from three times determination. Different letters on eah bar indiate signifiant differenes (P<0.05). D. Effet of Whey Protein Conentrate on Textural Properties of Washed Rohu Gel Fig. 4 shows the folding test and gel strength of washed kamaboko (K) and modori (M) gel of rohu ontaining WPC at different levels (0-3%). The onentration signifiantly affeted the gel strength in both of the modori and kamaboko gel (P<0.05). For modori gel, the folding test slightly inreased when ompared with the ontrol (P>0.05). No differene in folding test was found with further addition of WPC (P>0.05). The gel strength oinided with the folding test. The gel strength inreased with the addition of WPC (P<0.05). However, no signifiantly differene in gel strength was observed with the inrease in WPC above 1% (P>0.05). For kamaboko gel, no signifiant differene in folding test was observed (P>0.05). The gel strength inreased with the addition of 1% WPC (P<0.05), ompared with that of the ontrol. However, the addition of further WPC did not inrease the gel strength (P>0.05). This improvement of gel strength agreed with the findings of [5]. The addition of WPC improved the grade of bigeye snapper surimi from B to AA and enhaned the grade of threadfin bream surimi from B to A [5]. This may be due to the WPC having an inhibitory effet on the myofibrillar proteins of surimi or ating as an alternative substrate, whih dereases the proteolyti ativity [15]. The kamaboko gel had a higher folding test and the gel strength than the modori gel. This may be due to moleules of proteins unfolding slowly at 40 o C, and then interating with other moleules to form the threedimensional network. As the gel is heated at 90 o C, unfolded protein moleules beome ross-linked and a more ordered struture is formed, strengthening the gel [24]. In addition, gel set at 65 o C ould be affeted by the endogenous protease that remains within the myofibrillar protein after washing. Our results showed that washing Figure 4. Folding test (A) and gel strength (B) of washed rohu gels ontaining whey protein onentrate at various onentrations. standard deviation from five times determination. Different letters on eah bar indiate signifiant differenes (P<0.05). E. Effet of Whey Protein Conentrate on Expressible Water Content of Washed Rohu Gel Fig. 5 shows the expressible water ontent of washed kamaboko (K) and modori (M) gel of rohu at different levels of WPC (0-3%). For modori gel, no differene in expressible water ontent was observed with addition of 2017 Journal of Advaned Agriultural Tehnologies 229

5 Journal of Advaned Agriultural Tehnologies Vol. 4, No. 3, September 2017 further WPC (P>0.05). However, the expressible water ontent dereased with the addition of 1%WPC (P<0.05), ompared with that of the ontrol gel. The results agreed with those for gel strength. Moreover, these findings support the finding of [5], that the addition of WPC improved the water-holding apaity of lizardfish surimi. For kamaboko gel, the onentration of WPC did not signifiantly affet the expressible water ontent of the gel (P>0.05). This might be due to setting at 40oC followed by 90oC strengthening the gel network, whereas the addition of WPC had no signifiant effet b a b Whiteness Expressible water (%) 45 the washed mine already had a white olor, therefore the addition of WPC did not affet the olor. However, the result did not agree with those for the unwashed gel. Sine the lightness (L*) of the unwashed gel was less than that of the washed gel (Data not shown), the addition of the light ream olor WPC had a stronger effet on the olor of unwashed gels. b Conentration of WPC (%) 0 Figure 6. Whiteness of washed rohu gels ontaining whey protein onentrate at various onentrations. K is kamaboko gel and M is modori gel. IV. Conentration of WPC (%) Figure 5. Expressible water of washed rohu gels ontaining whey protein onentrate at various onentrations. standard deviation from three times determination. Different letters on eah bar indiate signifiant differenes (P<0.05). The results showed that the modori gel had a higher expressible water ontent than the kamaboko gel. These results oinided with those for the unwashed gel. A higher water-holding apaity was observed for the kamaboko gel network, whih may be due to the greater strength of the gel network set at 40oC. The unfolded protein moleules interated with eah moleule at 40oC, and then ross-linked to form an ordered struture at 90oC. These interations strengthened the gel network, whih retained more water [24], [27]. Moreover, the endogenous protease that remained within the myofibrillar protein might be ativated at 60 oc, degrading the three-dimensional network, and preventing an ordered struture forming at 90oC. Although WPC improved the modori gel at 1%, the water-holding apaity was not as high as that of kamaboko gel. This finding suggested that the addition of WPC at 1% ould improve the textural properties of modori gel Journal of Advaned Agriultural Tehnologies Our results onlude that the addition of WPC improves the textural properties and water-holding apaity of unwashed and washed rohu gel. The result for unwashed gel showed that the addition of WPC at 3% improved the modori gel, while the addition with 2%WPC improved the kamaboko gel, ompared with the ontrol. The result for the washed gel showed that the addition of WPC at 1% improved both gels. However, the inrease for either unwashed or washed modori gel was not as high as kamaboko gel. The addition of WPC affeted the whiteness of unwashed gel, but not affeted washed gel. ACKNOWLEDGMENT This study was finanially supported by the National Researh Counil of Thailand through Thammasat University for the 2017 fisal year. REFERENCES [1] [2] F. Effet of Whey Protein Conentrate on Whiteness of Washed Rohu Gel Fig. 6 shows the whiteness of washed kamaboko (K) and modori (M) gel of rohu at different levels of WPC (03%). For both of gels, the addition of WPC did not signifiantly affet the whiteness. This may be beause [3] 230 CONCLUSIONS National statistial offie of Thailand, 2014 Produts of freshwater fish farm. [Online]. Available: ojet-th.htm./ J. Phetploy, Frozen stability of musle protein from freshwater fish, M.S. thesis, Dept. Food Teh., Suranaree Univ of Teh., Nakhonrathasima, Thailand, 2005, [In Thai]. M. Kinoshita, H. Toyohara, and Y. Shimizu, Diverse distribution of four distint types of modori (gel degradation) - induing proteinases among fish speies, Nippon Suisan Gakk, vol. 56, pp , 1990.

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Teh, vol. 39, pp , [21] M. T. Morrissey, J. W. Wu, D. Lin, and H. An, Protease inhibitor effets on torsion measurements and autolysis of Paifi whiting surimi, J Food Si., vol. 58, pp , [22] S. Benjakul, K. Leelapongwattana, and W. Visessagnuan, Comparative study on proteolysis of two speies of bigeye snapper, Priaanthus maraanthus and Priaanthus tayenus, J Si. Food Agr., vol. 83, pp , [23] E. Niwa, T. T. Wang, H. Kanoh, and T. Nakayama, Contribution of gelling substane to musular protein network struture within kamaboko, Nippon Suisan Gakk, vol. 94, pp , [24] E. A. Foegeding, C. E. Allen, and W. R. Dayton, Effet of heating rate on thermally formed myosin, fibrinogen and albumin gels, J. Food Si., vol. 51, pp , [25] Y. Makinodan and S. Ikeda, Study on fish musle protease - IV. Relation between himodori of kamaboko and musle proteinase, Nippon Suisan Gakk, vol. 37, pp , [26] P. Suwansakornkul, Y. Itoh, S. Hara, and A. Obatake, The gel - forming harateristis of lizardfish, Nippon Suisan Gakk, vol. 59, pp , [27] T. Mahawanih, J. Lekhavihitr, and K. Duangmal, Gel properties of red tilapia surimi: Effets of setting ondition, fish freshness and frozen storage, Int. J. Food Si. Teh., vol. 45, pp , Phatthira Sutloet was born in Thailand on Marh 29 th, Eduational bakgrounds are listed as following: M.S. (Food Siene & Tehnology), Thammasat University, Thailand (2010) B.S. (Food Siene & Tehnology) (First Class Honor), Thammasat University, Thailand (2006) Currently, she is a Ph.D. student in Department of Food Siene and Tehnology, Thammasat University, Pathum Thani, Thailand. Her researh interest is mainly on fisheries siene. She has published artiles as following: (1) Prodution of rie noodle from gaba rie flour enrihment with fish protein, in Pro. 1 st National Rie Researh Conf. Moving rie researh towards innovation, Bangkok, 2010, pp (2). Use of edible seaweed extrats from Solieria robusta in Fish ball gel, J Si Teh, vol. 22(1), pp , (3) Effet of Grailaria fisheri extrat on harateristis of fish emulsion sausage, in Pro. 54th Kasetsart University Annu. Conf. Siene, Geneti Engineering, Arhiteture and Engineering, Agro- Industry, Natural Resoures and Environment, Bangkok, 2016, pp Warangkana Sompongse was born in Bangkok, Thailand. Eduational bakgrounds are listed as following: Ph.D. (Food Siene), The United Graduate Shool of Agriultural Sienes, Ehime University, Ehime, Japan (1996) M.S. (Aquati Produt Utilization), Kohi University, Kohi, Japan (1993) B.S. (Food Siene & Tehnology) (First Class Honor), Kasetsart University, Thailand (1990) She reeived a Japanese Government Sholarship (MONBUSHO) during her master and Ph.D. program. (Otober 1990-Marh 1996). After graduation, she was an instrutor in the Department of Food Siene and Tehnology, Faulty of Siene and Tehnology, Thammasat University, Thailand. She was granted by FY 2001, JSPS Postdotoral Fellowship for Foreign Researhers from November 2001to Otober Nowadays, she is an assoiate professor at the same institute. Current researh interests are fish protein and its denaturation, gelation of fish protein, utilization of fruit, vegetable and fish by-produts. Her publiations are as follows: (1) W. Sompongse, P. Phuphehr, and C. Nakju, Effet of Washing Conditions on Gelforming Ability of Short-bodied Makerel (Rastrelliger brahysoma) Ball with Green Curry Paste, presented at the IFT13 Annual Meeting, Illinois USA., July 13-16, (2) P. Sutloet and W. Sompongse. Effet of Grailaria fisheri Extrat on Charateristis of Fish Emulsion Sausage, in Pro. The 54th Kasetsart University Annu. Conf. Agro- Industry, February 2-5, Kasetsart University, Bangkok, 2016, pp (3) W. Sompongse, P. Teerasilvesakul and K. Seesaleekularat, Extration of Tamarind Seed (Tamarindus india L.) Gum by Mirowave and Its Appliation in Strawberry Jam, J Si Teh, vol. 24(2), pp , Dr. Sompongse is a senior member of the Asia-Paifi Chemial, Biologial & Environmental Engineering Soiety (APCBEES), and a member of the Food Siene and Tehnology Assoiation, Thailand (FoSTAT). She was reeived an award from registration of four pretty patents on the researher thank you day of Thammasat University, November 26, She was awarded from the 53th Kasetsart University Annual Conferene in the field of agro-industry on February 3-6, 2015 at Kasetsart University, Bangkok, for researh on Fators Affeting Gel Formation of Tamarind (Tamarindus india L.) Seed Gum. She reeived the best teaher award from Faulty of Siene and Tehnology, Thammasat University, Thailand on Marh 31, Journal of Advaned Agriultural Tehnologies 231

7 Journal of Advaned Agriultural Tehnologies Vol. 4, No. 3, September 2017 Katsuji Morioka was born in Osaka, Japan. Eduational bakgrounds are listed as following: Ph.D. in Agriulture, Kyoto University, Kyoto, Japan (1996) M.S. in Agriulture, Kyoto University, Kyoto, Japan (1987) B.S. in Agriulture, Kyoto University, Kyoto, Japan (1985) His employment history: Apr., Jan., 1999: Assistant Professor in Kohi University Feb., Apr., 2009: Assoiate Professor in Kohi University May, present: Professor in Kohi University, Kohi, Japan (Laboratory of Aquati Produt Utilization, Faulty of Agriulture). His publiations: (1) D.P. Thakur and K. Morioka, Comparison of ollagen distribution and musle struture between ultured amberjak (Seriola dumerili) and ultured yellowtail (Seriola quinqueradiata), J. Aquat Food Produt T, vol. 25, pp , (2) Y.Hu, K. Morioka, S. Chen, D. Liu, X. Ye, Effet of ied-storage on the ativity of athepsin L and trypsin-like protease in arp dorsal musle, LWT - Food Siene and Tehnology, vol. 60, pp , (3) Md.I. Hossain, K. Morioka, F. H. Shikha, and Y. Itoh, Effet of preheating temperature on the mirostruture of walleye pollak surimi gels under the inhibition of polymerization and degradation of myosin heavy hain, J Si Food Agri, vol. 91, pp , Current researh interests: (1) Quality assessment and improvement of ultured fish in Japan, (2) Effiient utilization of underutilized fish and fish by-produts. Professor Morioka is a member of Japanese Soiety of Fisheries Siene and is the editor of Fisheries Siene Journal of Advaned Agriultural Tehnologies 232