Proteoglycans and glycosaminoglycans were isolated from African night crawler (Eudrilus eugeniae Kinberg) and partially characterized proteoglycans (3.04 % of lyophilized worm) were liberated from the defatted and depurinated worm samples by dissociative method using 4M urea in acetate buffer. Glycosaminoglycans (12.47% of proteoglycan extract) were extracted using enzymatic hydrolysis of the proteoglycan extract with papain. Gel filtration chromatography using Sepharose CL-4B was used to purify and estimate the molecular weights of the proteoglycan and glycosaminoglycan fractions. Three proteoglycan fractions PGF1, PGF2 and PGF3 with estimated molecular weigths 860 kDa, 181 kDa and 3 kDa, respectively were identified as monitored by the Bradford and modified carbazole assay. Two glycosaminoglycan fractions -GF1 (MW = 860 kDa) and GF2 (MW=140 kDa) were identified using the modified carbazole assay. Infrared spectroscopy of the GF1 and GF2 showed the possible identities of the fractions. GF1 may be a hyaluronic acid and GF2 is possibly chondroitin. Anti-coagulant assay for the extracts and fractions revealed that the glycosaminoglycan isolate has anti-coagulant activity but not the GF1 and GF2 fractions individually.
Hypertension has been reported as the second major cause of morbidity in the Philippines. One of the mechanisms to control blood pressure is through the inhibition of the angiotensin I-converting enzyme (ACE). This study specifically focused on the determination of ACE inhibitory activities of peptides from ‘Carabao’ mango flesh of three shell colors (SC1, SC3, SC5). The bioactive peptides were obtained upon a series of extraction, purification, and enzymatic hydrolysis steps. Among the undigested and digested crude and purified samples, the highest in vitro ACE inhibition was exhibited by the three-hour digest of SC3 (83.28 ± 0.83%). The most prominent peak from the fractionation of the mixture of peptides in SC3 digest was evaluated for ACE inhibition, and the decrease in activity inferred the synergistic effect of the peptides in exhibiting the inhibitory function. This selected bioactive peptide was revealed to have alanine and phenylalanine as the components, which can possibly be AF – an ACE inhibitory peptide determined from in silico analyses. Meanwhile, assessment of the in vivo antihypertensive activity showed no significant results due to insufficiently administered doses of the samples. Overall, the measured activity of the ACE inhibitory peptides inferred the potential of mango as a functional food in dealing with hypertension.
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