The Functional Properties of Buffalo skin Gelatin Extracted Using Crude Acid Protease from Cow’s Abomasum

Abstract

The study was investigated the functional properties of buffalo skin gelatine. Gelatine was extracted from swamp buffalo skin using crude acid protease from cow’s abomasum (CAPC) in concentration variation 0; 2.5; 5; and 7.5 U/mg. The temperature to hydrolysis included at 28 °C, 37°C and 40°C. The emulsion activity index (EAI), Emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS) were investigated. The interaction between CAPC concentration and hydrolysis temperature has a significant effect (P <0.05) on the emulsion activity index (EAI), emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS). The highest EAI was obtained in CAPC concentration of 5 U /mg, hydrolysis temperature of 40°C, which was 12.04 m2/g. The higher concentration of CAPC decreased the ESI. The hydrolysis temperature of 40°C produces higher FE than 28°C and 40°C. The highest FE is obtained at CAPC 5U/mg, 37°C hydrolysis temperature, which is 102.93%. The FS values range from 44.91-55.00%. This value is higher than commercial gelatin (bovine skin gelatin) which is 34.90%. The conclusion of this study is that buffalo skin gelatin with the best functional properties was obtained using CAPC 5 U/mg, the hydrolysis temperature of 40°C.

Characterisation of gelatin extracted from buffalo (Bubalus bubalis) bone using papain pre-treatment

“…Whereas the foam stability for NE was (13.33 ± 1.15 %) and PE (13.00 ± 1.00 %) at 30 min, while at 60 min, PE (12.67 ± 1.53 %) and NE (11.33±0.58 %) showing no significant difference (p > 0.05). Mulyani et al (2019) reported a higher FE (102.93 %) and FS (44.91-55.00 %) value compared to the result of this study. The study by Khiari et al (2013), of enzymatically extracted fish gelatin, resulted in more stable foam as compared to NE due to high negatively charged amino acids in the gelatin.…”

“…There was no significant difference observed for both samples (p > 0.05). The EAI value or NE was similar to gelatin extracted by Mulyani et al (2019) (12.03 m 2 /g). In contrast, PE was slightly lower as compared to Mulyani et al (2019) for gelatin extracted from buffalo skin.…”

“…The EAI value or NE was similar to gelatin extracted by Mulyani et al (2019) (12.03 m 2 /g). In contrast, PE was slightly lower as compared to Mulyani et al (2019) for gelatin extracted from buffalo skin. Meanwhile, for the ESI value, PE (30.05 ± 0.38 min) was significantly higher than that of NE (3.76 ± 0.74 min).…”

“…Meanwhile, for the ESI value, PE (30.05 ± 0.38 min) was significantly higher than that of NE (3.76 ± 0.74 min). Moreover, the ESI value of PE and NE was much lower than gelatin extracted from cow bone using crude acid protease cow Mulyani et al (2019). Here, the EAI was mainly influenced by the variations in intrinsic properties, protein conformation, in addition to the composition of amino acids (Zilhadia et al, 2018).…”

The Influence of the Structure of Selected Polymers on Their Properties and Food-Related Applications

“…Gelatine is also used in confectionery due to its foaming ability, for example in marshmallow production [ 123 ]. Foaming increases with the amount of hydrophobic amino acids such as alanine, valine, isoleucine, leucine, proline, methionine, phenylalanine, tyrosine, and tryptophan, as hydrophobicity is a requirement for adsorption at the air–water interface [ 124 ].…”