Gel-Forming Ability of Mackerel (Rastrelliger Branchysoma) Protein Isolate as Affected by Microbial Transglutaminase


  • Manat CHAIJAN Division of Food Technology, School of Agricultural Technology, Walailak University, Nakhon Si Thammarat 80161
  • Worrawan PANPIPAT Division of Food Technology, School of Agricultural Technology, Walailak University, Nakhon Si Thammarat 80161


Short-bodied mackerel, protein isolate, gel-forming ability, microbial transglutaminase


The properties of gel from short-bodied mackerel (Rastrelliger branchysoma) alkaline-solubilized protein isolate with different levels (0, 0.25, 0.5, 1.0 and 1.5 unit/g sample) of microbial transglutaminase added (MTGase) and subjected to setting at 40 °C for 30 min, prior to heating at 90 °C for 20 min were investigated. The breaking force of the protein isolate gels with MTGase added at all levels was higher than that of the control gel (without the addition of MTGase) (p < 0.05). However, the increase in the amount of MTGase added had no effect on the breaking force of protein isolate gels (p > 0.05). From the result, no changes in deformation in all gels treated with and without MTGase were noticeable (p > 0.05). The lowest expressible moisture was found in the gel with 0.25 unit/g of MTGase (p < 0.05). Generally, the whiteness of all gels incorporating MTGase were lower than that without MTGase (p < 0.05). Therefore, the addition of MTGase at 0.25 unit/g sample in combination with an appropriate heating regime was a promising means to improve the gel properties, especially strength and water holding capacity, of short-bodied mackerel protein isolate prepared by alkaline solubilization.


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Y Shimizu, H Toyohara and TC Lanier. Surimi Production from Fatty and Dark-Fleshed Fish Species. In: TC Lanier and CM Lee (eds.). Surimi Technology. Marcel Dekker, New York, 1992, p. 181-207.

Y Ochiai, L Ochiai, K Hashimoto and S Watabe. Quantitative estimation of dark muscle content in the mackerel meat paste and its products using antisera against myosin light chains. J. Food Sci. 2001; 66, 1301-5.

HO Hultin and SD Kelleher. Surimi Processing from Dark Muscle Fish. In: JW Park (ed.). Surimi and Surimi Seafood. Marcel Dekker, New York, 2000, p. 59-77.

KE Spencer and MA Tung. Surimi Processing from Fatty Fish. In: F Shahidi and JR Botta (eds.). Seafood: Chemistry, Processing Technology and Quality. Chapman & Hall, New York, 1994, p. 288-319.

M Chaijan, S Benjakul, W Visessanguan and C Faustman. Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand. Food Res. Int. 2004; 37, 1021-30.

I Undeland, SD Kelleher and HO Hultin. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J. Agric. Food Chem. 2002; 50, 7371-9.

HG Kristinsson and R Ingadottir. Recovery and properties of muscle proteins extracted from tilapia (Oreochromis niloticus) light muscle by pH shift processing. J. Food Sci. 2006; 71, 132-41.

J Yongsawatdikul and JW Park. Effect of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins. J. Food Sci. 2004; 69, 499-505.

M Perez-Mateos, PM Amato and TC Lanier. Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization. J. Food Sci. 2004; 69, 328-33.

YS Kim, JW Park and YJ Choi. New approaches for the effective recovery of fish proteins and their physicochemical characteristics. Fisheries Sci. 2003; 69, 1231-9.

M Chaijan, S Benjakul, W Visessanguan and C Faustman. Physicochemical properties, gel-forming ability and myoglobin content of sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) surimi produced by conventional method and alkaline solubilization process. Eur. Food Res. Tech. 2006; 222, 58-63.

M Perez-Mateos and TC Lanier. Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization. Food Chem. 2006; 101, 1223-9.

S Rawdkuen, S Sai-Ut, S Khamsorn, M Chaijan and S Benjakul. Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process. Food Chem. 2009; 112, 112-9.

NF Haard BK Simpson and BS Pan. Sarcoplasmic Proteins and Other Nitrogenous Compounds. In: ZE Sikorski BS Pan and F Shahidi (eds.).Seafood Proteins. Chapman & Hall, New York, 1994, p. 13-39.

ZE Sikorski. The Myofibrillar Proteins in Seafoods. In: ZE Sikorski BS Pan and F Shahidi (eds.). Seafood Proteins. Chapman & Hall, New York, 1994, p. 40-57.

N Nio, M Motoki and K Takinami. Gelation mechanism of protein solution by transglutaminase. Agric. Biol. Chem. 1986; 50, 851-5.

M Nonaka, S Toiguchi, H Sakamoto, H Kawajiri, T Soeda and M Motoki. Changes caused by microbial transglutaminase on physical properties of thermal induced soy protein gels. Food Hydrocolloids. 1994; 8, 1-8.

H Sakamoto, Y Kumazawa, S Toiguchi, K Seguro, T Soeda and M Motoki. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. J. Food Sci. 1995; 60, 300-4.

L Kurth and PJ Rogers. Transglutaminase catalyzed cross-linking of myosin to soy protein, casein and gluten. J. Food Sci. 1984; 49, 573-89.

SH Kim, JA Crapenter, TC Lanier and L Wicker. Polymerization of beef actomyosin induced by transglutaminase. J. Food Sci. 1993; 58, 473-91.

C Kuraishi, J Sakamoto, K Yamazaki Y Sosa, C Kuhara and T Soeda. Production of restructured meat during microbial transglutaminase without salt or cooking. J. Food Sci. 1997; 62, 488-515.

HG Lee, TC Lanier, DD Hamann and JA Knopp. Transglutaminase effects on low temperature gelation of fish proteins sols. J. Food Sci. 1997; 62, 20-3.

U Gerber, U Jucknischke, S Putzien and HL Fuchsbauer. A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense. J. Biochem. 1994; 229, 825-9.

YP Huang, K Seguno, M Motoki and K Tawada. Cross-linking of contractile proteins from skeletal muscle by treatment with microbial transglutaminase. J. Biochem. 1992; 112, 229-34.

K Washizu, K Ando, S Koikeda, S Hirose, A Matsuura and H Takagi. Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans. Biosci. Biotech. Biochem. 1994; 58, 82-7.

M Faergemand, O Otte and KB Quist. Enzymatic cross-linking of whey proteins by a Ca2+-independent microbial transglutaminase from Streptomyces ludicus. Food Hydrocolloids. 1997; 11, 19-25.

MI Ho, SZ Leu, JE Hsieh and ST Jiang. Technical approach to simplify the purification method and characterization of microbial transglutaminase produced from Streptoverticillium ladakanum. J. Food Sci. 2000; 65, 76-80.

C Nakahara, H Nozawa and N Seki. A comparison of cross-kinking of fish myofibrillar proteins by endogenous and microbial transglutaminases. Fisheries Sci. 1999; 65, 138-44.

M Nonaka, H Tanaka, A Okiyama, M Motoki, H Ando and K Umeda. Polymerization of several proteins by Ca2+-independent transglutaminase derived from microorganism. Agric. Biol. Chem. 1989; 53, 2619-23.

H Tanaka, M Nonaka and M Motoki. Polymerization and gelation of carp myosin by microbial transglutaminase. Nippon Suisan Gakk. 1990; 56, 1341-7.

JE Folk. Transglutaminase. Method Enzymol. 1970; 17, 889-94.

JW Park. Functional protein additives in surimi gels. J. Food Sci. 1994; 59, 525-7.

CS Ng. Measurement of Free and Expressible Drips. In: H Hasegawa (ed.). Manual on Analytical Methods and Procedure for Fish and Fish Products Laboratory. Southeast Asian Fisheries Development Center, Singapore, 1978, p. 1-2.

RGD Steel and JH Torrie. Principle and Procedure of Statistics. 2nd ed. MacGraw-Hill, New York, 1980.

IM Kimura, M Sugimoto, K Toyoda, N Seki, K Arai and T Fujita. A study on the cross-linking of myosin in kamaboko “suwari” gels. Nippon Suisan Gakk. 1991; 57, 1386-96.

A Tammatinna, S Benjakul, W Visessanguan and M Tanaka. Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase. LWT. 2007; 40, 1489-97.

N Seki, H Uno, NH Lee, I Kimura, K Toyoda and T Fujita. Transglutaminase activity in Alaska Pollack muscle and surimi, and its reaction with myosin B. Nippon Suisan Gakk. 1990; 56, 125-32.

ST Jiang, JF Hsieh, ML Ho and YC Chung. Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollack surimi. J. Food Sci. 2000; 65, 694-9.

K Seguro, Y Kumazawa, T Ohtsuka, S Toiguchi and M Motoki. Microbial transglutaminase -(-glutamyl) lysine crosslink effects on elastics properties of kamaboko gels. J. Food Sci. 1995; 60, 305-11.

GJ Tsai, SM Lin and ST Jiang. Transglutaminase from Streptoverticillium ladakanum and application to mince fish product. J. Food Sci. 1996; 61, 1234-8.

T Asakami, M Ogiwara, A Wakameda and S Nogushi. Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species. Fisheries Sci. 1995; 61, 267-72.

Y Matsumura, Y Chanyonguorakul, Y Kamazawa, T Ohtsuka and T Mori. Enhanced susceptibility to transglutaminase reaction of -lactoglobulin in the molten globule state. Biochim Biophys. Acta. 1996; 1249, 69-76.

E Niwa. Chemistry of Surimi Gelation. In: TC Lanier and CM Lee (eds.). Surimi Technology. Marcel Dekker, New York, 1992, p. 389-427.

M Chaijan, S Benjakul, W Visessanguan, S Lee and C Faustman. The effect of freezing and aldehydes on the interaction between fish myoglobin and myofibrillar proteins. J. Agric. Food Chem. 2007; 55, 4526-8.




How to Cite

CHAIJAN, M., & PANPIPAT, W. (2011). Gel-Forming Ability of Mackerel (Rastrelliger Branchysoma) Protein Isolate as Affected by Microbial Transglutaminase. Walailak Journal of Science and Technology (WJST), 7(1), 41–49. Retrieved from



Research Article