Green tea leaves as a source of natural antioxidants has a huge potential to improve sausage quality from lamb meat, in line with an increase of people concern in functional food products. This study aimed to evaluate inclusion of green tea leaves (Camelia sinensis) powder (GTP) into lamb sausage on physicochemical properties, total microbes, oxidative stability, and sensory quality. Three lambs aged one year was slaughtered as sausage meat source. Incorporation of 0.0%, 1.0%, 1.5%, and 2.0% GTP to lamb sausage during 0, 7, and 14 days of storage was conducted in a completely randomized design of ANOVA with five replications in each treatment. Few changes were observed on chemical and physical qualities by adding 1% GTP, particularly on protein and water holding capacity (WHC) (p<0.05), while moisture, fat, pH, and tenderness were not affected (p>0.05). Lipid oxidation and the number of total plate count (TPC) were reduced by 36%-40% and 31%-49%, respectively by the inclusion of 1% GTP during storage time (p<0.05). Adding GTP negatively affected the sensory quality of lamb sausage since the score of acceptability reduced in the group of sausages contained GTP although the scores for color, flavor, and odor were higher with GTP addition. The incorporation of GTP was effectively inhibiting bacterial growth and lipid oxidation in the lamb sausage. However, GTP was also ineffective at improving the sensory quality of the sausage.

The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE). This research was conducted in three replications, with the measured parameters include ACE inhibitory potential and collagen hydrolysate fractionation. The results showed that collagen extraction of Kacang goat skin by chymotrypsin hydrolysis yielded 9.74% (dry matter, v/v) collagen, with pH at 6.6. The extracted collagen contained α1, α2, and β collagen chains with molecular weights of 151 kDa, 141 kDa, and 240 kDa, respectively. Furthermore, the collagen hydrolysis produced protein peptides confirmed at molecular weights of 43 to 107 kDa. The hydrolysate fractionation at molecular weights of <3 kDa, 3-5 kDa, and >5 kDa showed proteins concentrations of 2.33 mg/mL, 3.81 mg/mL, and 3.93 mg/mL, respectively. The hydrolysate fractionation with molecular weight <3 kDa showed to have ACE inhibition activity with the IC50 value of 0.47 mg/mL. The study concluded that collagen hydrolysate extracted from the skin of Kacang goat had a promising potential as a source of antihypertensive agent.

Background and Aim: Angiotensin-converting enzyme (ACE) is one of the inhibitory enzymes isolated from animals for the treatment of hypertension. ACE inhibitor (ACE-I) peptides can be obtained by hydrolyzing proteins from various animal tissues, including muscle and connective tissues. However, the study on ACE-I activity from collagen of Kacang goat skin has not been conducted. This study explores the potency of collagen from Kacang goat skin as a source of an antihypertensive agent through ACE inhibition. Thermolysin will hydrolyze collagen and produce the peptide classified antihypertensive bioactive peptides. This study aimed to determine the potential of thermolysin to hydrolyze collagen of Kacang goat skin for ACE-I peptide production and to identify the production of ACE-I peptides. Materials and Methods: Collagen from Kacang goat skin was hydrolyzed with thermolysin and incubated at 37°C for 1 h. Molecular weight (MW) evaluation was performed by SDS PAGE; fractionation peptides at <5 kDa, 3-5 kDa, and <3 kDa were performed by ultrafiltration and ACE-I activity determined by IC50 measurement. Results: Collagen was hydrolyzed by thermolysin, resulting in protein with MW of 117.50-14.60 kDa. The protein content of fractionation at >5 kDa was 3.93±0.72 mg/mL, content of 3-5 kDa was 3.81±0.68 mg/mL, and that of <3 kDa was 2.33±0.38 mg/mL. Fractionation was performed 3 times and one of the results was selected for the ACE-I test. The selected fraction was tested by IC50 measurement with three repetitions and it showed an average enzyme activity at 0.83 μg/mL or 82.94 mg/mL. Conclusion: Thermolysin hydrolysis of collagen from Kacang goat skin showed the potential to produce bioactive peptides, such as ACE-I.

Red beetroot is rich in phenolic acids and betalain as natural food-coloring agents. Freeze-dried red beetroot that ground into powder can be used as a source of natural coloring to substitute the use of synthetic food color additives as well as filler to substitute tapioca. This study evaluates the function of red beetroot powder not only as filler but also as coloring agent on chicken sausage. Furthermore, its effects as filler (tapioca and beetroot) were also observed on the physical and sensory characteristics of the produced chicken sausage. The substitution of tapioca flour and beetroot powder in this study were 18:0, 17:1, 16:2, and 15:3 (%:%). Each treatment was consisted of three replications. The examined physical properties include pH, water-holding capacity (WHC) and sensory properties. The study found that WHC, color, texture profile and sensory properties were influenced by the increasing level of beetroot flour ratio, while different ratios had no effect on the pH. Chicken sausages made with higher ratio of beetroot flour had good acceptability on flavor and color. The conclusions of this study were substitution tapioca with 2% beetroot powder influenced physical quality (water holding capacity and tenderness) and sensory (color and flavor) of chicken sausage.

This research aimed to investigate the rabbit meat hydrolysate potential as an angiotensin-converting enzyme (ACE) inhibitor. Indonesian local rabbit meats were used in this study. The research was conducted in Department of Animal Product Technology, Faculty of Animal Science, Universitas Gadjah Mada, from August 2016 to February 2017. The local rabbit meats were hydrolyzed by pepsin, trypsin, and pancreatic. The obtained hydrolysates were then analyzed to identify the water-soluble protein content. The molecular weight of the hydrolysates were also confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The ACE inhibitory properties of the hydrolysates were analyzed in vitro. The results showed that pepsin, trypsin, and pancreatic hydrolysis showed a significant effect on the water-soluble protein content of rabbit meat (p<0.05). The water-soluble protein of rabbit meat hydrolysed by pepsin, trypsin, and pancreatic were 9.41, 7.66, and 9.75 mg/mL respectively. The molecular weight of the rabbit meat hydrolysate were increased from 10 to 43 kDa; 17 to 43 kDa; and 10 to 43 kDa, after hydrolysed by by pepsin, trypsin, and pancreatic respectively. Furthermore, the ACE inhibitory properties ) of the hydrolysed rabbit meat by pepsin, trypsin, and pancreatic were 439, 170, and 380 μg/mL, respectively. The rabbit meat hydrolysate showed a potential to be ACE inhibitor after hydrolyzed with pepsin, trypsin and pancreatic. Moreover, it also showed a promising potential to be used as bioactive components in different pharmaceutical applications. The highest ACE inhibitory capability was showed on trypsin hydrolysis with the total of 65.45% and 170 μg/mL ACE inhibition