Bakteri Asam Laktat Lactobacillus Plantarum C410LI dan Lactobacillus Rossiae LS6 yang Diisolasi dari Lemea Rejang terhadap Suhu, pH dan Garam Empedu Berpotensi sebagai Prebiotik

Based on previous research it was found that lemea (traditional food rejang) was proven to contain 2 types of lactic acid bacteria (BAL) namely L.aplantarum C410L1 and L. crossiae LS6 which could be probiotic and beneficial for health. The development of lemea as a potential probiotic must be proven its resistance to bile acids and salts as an indication of being able to survive in the gastrointestinal tract. This study aims to determine the resistance of BAL isolated from lemea against low pH, bile acids, and temperature. This research is an experimental study with all research units controlled. Analysis of BAL resistance to high temperatures, low pH, and bile salts was carried out in the Bengkulu Polytechnic Health Polytechnic laboratory. The total BAL colonies increased at 49 ° C and decreased at 64 ° C. The increase in the total number of BAL colonies within 0-30 hours occurred at pH 5 and pH 6. There was no increase or decrease in the total number of BAL colonies in salts 0.30%, 0.60%, and 0.90%. The diisolate lactic acid (BAL) bacteria from lemea have a temperature resistance of 42 ° C to 64 ° C, pH 2 to pH 7, have a salt resistance concentration of 0.30% to 0.90%. Lactic acid bacteria (BAL) which are diisolate from lemea have the potential as probiotics.

A low-molecular-weight protein from rat liver that resembles ligandin in its binding properties

A protein of S20,W 1.6S and mol.wt. 14000, which binds covalently a metabolite of the aminoazodye carcinogen NN-dimethyl-4-amino-3′-methylazobenzene, was isolated from rat liver cytosol from both carcinogen-treated and normal rats. The protein binds non-covalently palmitoyl-CoA, fatty acids, bilirubin, sex steroids and their sulphates, bile acids and salts, bromosulphophthalein, diethylstilboestrol and 20-methylcholanthrene with a wide range of affinities. The protein is isolated as three components with isoelectric points of 5.0, 5.9 and 7.6 by a method involving isoelectric focusing. All three components have closely similar amino acid analyses, tryptic-peptide ‘maps’ and u.v. spectra. Each single component redistributes into all three on further electrophoresis. However, the three forms differ in their binding characteristics, the form of pI 7.6 having much the highest affinity for compounds bound non-covalently. The protein was identified immunologically in rat liver, small intestine, adipose tissue, skeletal muscle, myocardium and testis. The protein was compared with other hepatic binding-protein preparations of similar molecular weight.

A Direct Enzymic Assay for 7α-Hydroxy Bile Acids and Their Conjugates

1. A 7α-hydroxysteroid dehydrogenase preparation isolated from a strain of Escherichia coli provides a specific and rapid means for the determination of 7α-hydroxy bile acids and their conjugates. 2. When used in conjunction with 3α-hydroxysteroid dehydrogenase the method enables the concentrations of primary and secondary bile acids and salts in biological fluids to be determined directly without the use of thin-layer chromatography. 3. When used with thin-layer chromatography the method allows the specific quantitative determination of chenodeoxycholic acid or its conjugates in the presence of deoxycholic acid and its derivatives.