![]() ![]() Our findings suggest that recreational beaches may contribute to the dissemination of Enterococci with HLAR and virulence characteristics. Suggestively, these are the main virulent characteristics of the studied beach Enterococci. Analysis of obtained spearman's coefficient showed a strong correlation between caseinase and each of the slime production (p = 0.04), gelatinase (p = 0.0035) and haemolytic activity on horse blood (p = 0.004), respectively. A strong association was observed between the source of isolation and responses for each of caseinase (C = 0.47, V = 0.53) and slime (C = 0.50, V = 0.58) assays. On the whole, caseinase production was profoundly highest (15.01 %) while the least prevalent virulence characteristic observed among tested beach Enterococci was haemolysis of rabbit blood (3.65 %). A total of 160 isolates were also tested for virulence characteristics. The species classification of encountered Enterococci resistance to vancomycin was highest among Enterococcus spp. Chi-square analysis showed no significant association between responses to tested antibiotics and the species allocation or source of isolation of all tested Enterococci. High-level resistance to kanamycin was higher among Enterococcus faecalis and Enterococcus faecium than Enterococcus spp. However, high-level resistance to kanamycin (2,000 μg/mL) was observed in 14.2 % of tested isolates, the highest proportions observed being among beach sand isolates. None of the encountered isolates were resistant to high levels of gentamicin (500 μg/mL). We report the first study on the occurrence of high-level aminoglycoside-resistant (HLAR) Enterococci in coastal bathing waters and beach sand in Malaysia. Strain G6 bacterium showed greatest gelatinase activity towards porcine gelatine which can be potentially used for porcine gelatine identification. Application of partially purified gelatinase onto porcine, bovine and fish capsules substituted into the gelatin medium (GM), respectively resulted in 11.86 a ± 0.2 U/ml, 5.39 b ± 2.1 U/ml and 0.36 c ± 0.2 U/ml of enzyme activity, respectively. The molecular weight of gelatinase of Strain G6 was 123.35 kDa. The partially purified gelatinase of Strain G6 showed significant different (p<0.05) in porcine gelatinase activity of 9.12 a ± 2.6 U/ml followed by bovine (5.43 b ± 0.8 U/ ml) and fish gelatine (0.14 c ± 0.7 U/ml). Gelatinase from the bacterium has been partially purified using deposition of ammonium sulphate and tube dialysis. Meanwhile, by using Biolog GEN III, the bacterium strain was identified as Lysinibacillus sphaericus analysis at 42% of similarity. Strain G6 using the partial sequence of 16S rDNA analysis with 95% of similarity. The bacterium was identified as Lysinibacillus spp. The Strain G6 colony was chosen due to its high ability to hydrolyse porcine gelatine when it was grown on medium containing porcine gelatine by forming a clear zone. (Strain G6) for hydrolysing porcine gelatine. This study indicated that animal waste like hoofs can be converted to useful gelatin hydrolysate using microbial gelatinase and used for various applications.This study was conducted to identify and characterize gelatinase bacterium of Lysinibacillus spp. The hydrolysis has maximum activity at 4 h incubation period and at a high amount of enzyme concentration. The production process for the gelatin hydrolysis was optimized by varying enzyme concentration and incubation time. The enzyme was used to produce gelatin hydrolysate by hydrolyzing animal hooves. The isolate produced more enzymes with the addition of peptone as a nitrogen source. ![]() ![]() The optimum enzyme production under solid-state fermentation includes an incubation period of 120 h and a moisture content of 66.7%. Gelatinase was optimally active at a temperature of 50☌ and at pH 8. The organism can grow under solid-state fermentation and produce gelatinase enzyme with a high activity using wheat bran as a carbon source. One isolate was selected for further analysis based on the eminent properties of the enzymatic reaction. All isolates were screened for the production of gelatinase on gelatin-containing media. A total of 100 bacterial isolates were isolated from soil and water samples. This study aimed to isolate the gelatinase enzyme from bacteria and optimize the reaction condition for gelatin hydrolysis. In recent years gelatin hydrolysates have gained a considerable indication in the applications of food and non-food products. Gelatinases are enzymes used to hydrolyze gelatin into peptides and amino acids. Enzymatic hydrolysis of gelatin increases its functional, textural, and nutritional characteristics. ![]()
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