Influence of Transglutaminase‐Induced Cross‐Linking on Properties of Fish Gelatin Films

Abstract

Fish gelatin (FG) is a potential alternative to current mammalian (beef and pork) gelatin. However, its physical and thermal properties limit its use in many applications. The treatment of microbial transglutaminase (MTGase) on FG could be a practical way to increase the use of FG films in various applications. Physical properties, barrier properties, and molecular weight change of FG films were measured. The viscosity of the MTGase‐treated FG solution significantly (P < 0.05) increased from 6.81 ± 0.65 cP to 35.04 ± 3.59 cP as the reaction time and concentration of MTGase increased. After employing 2% of MTGase into FG solution, the tensile strength increased from 48.03 ± 5.45 MPa to 68.00 ± 1.9 MPa, while percent elongation decreased from 13.1%± 2.90% to 1.47%± 0.05%. Oxygen barrier property was significantly (P < 0.05) increased from 7.24 ± 1.48 cc·m/m2·d to 17.69 ± 3.08 cc·m/m2·d, while water vapor permeability was not statistically (P < 0.05) different. The melting temperature (Tm) measured by differential scanning calorimetry increased from 124.78 ± 1.98 °C to 158.49 ± 2.68 °C as the enzyme reaction time increased. The color values of L*, a*, and b* were changed from 95.56 ± 0.09 to 95.50 ± 0.06, from −0.17 ± 0.01 to −0.23 ± 0.00, and from 3.17 ± 0.04 to 3.47 ± 0.09, respectively. The opacity significantly (P < 0.05) increased from 1.43%± 0.32% to 2.87%± 0.06%. SDS‐PAGE results showed that the molecular weight of fish gelatin films increased when the MTGase reaction takes place.

The Properties of Edible Film Derived From Bovine Split Hide Gelatin With Isolated Soy Protein Using Various Levels of Glycerol in the Presence of Transglutaminase

“…These compounds will be absorbed intensively to form hydrogen bonds with water (Nieto, 2009). Yi et al (2006) reported that the increase in the degree of isolated soy protein of gelatin films of fish caused by increased transglutaminase enzyme treatment, from 6.80% to 32.59%. The enzymatic cross-linked could cause an increase in molecular weight fish gelatin (Gomez-Guillen et al, 2001).…”

Perspectives on the Utilization of Aquaculture Coproduct in Europe and Asia: Prospects for Value Addition and Improved Resource Efficiency

“…However, a major application of gelatines has been in chilled desserts which could perhaps favour lower melting point fish gelatines because of better release of flavours and aromas (Choi and Regenstein 2000;Boran et al 2010) and offer alternative product options because of different textures and properties . Some additives such as neutral salts (Sarabia et al 2000), sugars (Choi and Regenstein 2000), egg albumen (Badii and Howell 2006) or treatments with 27 transglutaminase (Yi et al 2006) may improve properties but uncertainty exists over the halal status of enzyme treatments (Karim and Bhat 2009). …”

“…Other applications include possible biomedical uses such as biocompatible films and fibres with similar properties to collagen, possibly combined with other biopolymers such as chitosan, described below (Yi et al 2006). The most desirable qualities for all applications are high gel strength, viscosity and rheological properties, given particularly by the amino/imino acid contents and lower content of low molecular weight fractions (Karim and Bhat 2009;Eysturskarð et al 2009;Badii and Howell 2006) but also higher gelatine concentration and maturation temperature, i.e.…”

Water resistance and mechanical property improvement of tilapia (Tilapia zillii) scale gelatin films by dehydrated thermal treatment

“…Consequently, several studies have been carried out with an attempt to improve the performance of gelatin films by addition of cross-linking agents such as aldehydes (Bigi et al 2001), transglutaminase or 1-ethyl-3-(3-dimethylamino-propyl) carbodiimide (Kołodziejska and Piotrowska 2007;Yi et al 2006). However, the toxicity and high cost of some agents have limited their practical application.…”