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M.N. Cahyanto
Faculty of Agricultural Technology, Gadjah Mada University, Jl. Flora No.1 Bulaksumur, Yogyakarta 55281
Agriculture, Biological Sciences & Forestry Earth & Planetary Sciences

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COMPARATIVE STUDY ON ANGIOTENSIN CONVERTING ENZYME INHIBITORY ACTIVITY OF HYDROLYSATE OF MEAT PROTEIN OF INDONESIAN LOCAL LIVESTOCKS Jamhari, J.; Yusiati, L.M.; Suryanto, E.; Cahyanto, M.N.; Erwanto, Y.; Muguruma, M.
Journal of the Indonesian Tropical Animal Agriculture Vol 38, No 1 (2013): (March)
Publisher : Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14710/jitaa.38.1.27-33

Abstract

The experiment was conducted to investigate the angiotensin converting enzyme (ACE) inhibitoryactivity of hydrolysate in meat protein of Bali cattle, Kacang goat, native chicken, and local duck. Themeats of Bali cattle, Kacang goat, native chicken, and local duck were used in this study. The meatswere ground using food processor added with aquadest to obtain meat extract. The meat extracts werethen hydrolyzed using protease enzymes to obtain hydrolysate of meat protein. Protein concentration ofmeat extract and hydrolysate of meat protein were determined, and were confirmed by sodium dodecylsulfate - poly acrylamide gel electrophoresis (SDS-PAGE). ACE inhibitory activity of hydrolysate ofmeat protein derived from Bali cattle, Kacang goat, native chicken, and local duck was also determined.The results showed that protein concentration of hydrolysate of meat protein of Bali cattle, Kacang goat,native chicken, and local duck meat was significantly higher than their meat extracts. SDS-PAGEanalysis indicated that hydrolysate of meat protein of Bali cattle, Kacang goat, native chicken, and localduck had more peptides with lower molecular weight, compared to their meat extracts. Hydrolysate ofmeat protein of Bali cattle, Kacang goat, native chicken, and local duck had potencies in inhibiting ACEactivity, so it will potentially reduce blood pressure.
PURIFICATION OF ANGIOTENSIN CONVERTING ENZYME INHIBITORY PEPTIDE DERIVED FROM KACANG GOAT MEAT PROTEIN HYDROLYSATE Jamhari, J.; Yusiati, L.M.; Suryanto, E.; Cahyanto, M.N.; Erwanto, Y.; Muguruma, M.
Journal of the Indonesian Tropical Animal Agriculture Vol 38, No 4 (2013): (December)
Publisher : Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14710/jitaa.38.4.239-246

Abstract

The objective of this study was to identify the Angiotensin Converting Enzyme (ACE) inhibitorypeptide derived from Kacang goat meat protein hydrolysate. Kacang goat meat loin section washydrolyzed with pepsin, trypsin and chymotrypsin. Protein hydrolysate of Kacang goat meat was thentested the protein concentration and ACE inhibitory activity. ACE inhibitory peptide of the proteinhydrolysate was purified through several steps of purification by column SEP-PAK Plus C18 Cartridgeand RP-HPLC using a Cosmosil column 5PE-SM, 4.6 x 250　mm. The sequence of amino acid of ACEinhibitory peptide was identified by amino acid sequencer. The results showed that amino acidssequence of ACE inhibitory peptide derived from protein hydrolysate of Kacang goat meat was leu-thrglu-ala-pro-leu-asn-pro-lys-ala-arg- asn-glu-lys. It had a molecular weight (MW) of 1581 and occurredat the position of 20th to 33rd residues of b-actin of goat meat protein (Capra hircus). The ACE inhibitoryactivity (IC50) of the peptide was 190 mg/mL or 120 mM.
POTENCY OF LIGNOCELLULOSE DEGRADING BACTERIA ISOLATED FROM BUFFALO AND HORSE GASTROINTESTINAL TRACT AND ELEPHANT DUNG FOR FEED FIBER DEGRADATION Wahyudi, A.; Cahyanto, M.N.; Soejono, M.; Bachruddin, Z.
Journal of the Indonesian Tropical Animal Agriculture Vol 35, No 1 (2010): (March)
Publisher : Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14710/jitaa.35.1.34-41

Abstract

Lignin is limiting factor for cellulose and hemicellulose degradation in rumen. Isolation andselection bacteria from buffalo and horse gastrointestinal tract and elephant dung could be foundbacteria that have superiority to degrade lignin, xylan, and cellulose. Those animals were chosenbecause they were herbivores that consume low quality crude fiber as their main energy sources.Lignocellulose degrading bacteria were isolated by Hungate selective media, by using lignin (tannicacid), xylan, and cellulose as selective substrates. The morphological identification used an enrichmentmedia by measuring color, colony size, diffusion zone, clear zone, and biochemical identification usingproduction of ligninase, xylanase, and cellulase enzymes. The best lignocellulose degrading bacteriathen was determined by the morphological and biochemical character. This study showed thatlignocellulose degrading bacteria could be found in gastrointestinal tract of buffalo and horse, andelephant dung. Highest number colony was found in samples from buffalo's colon (376), followed byhorse's cecum (203), elephant’s dung (46), buffalo’s cecum (23), buffalo's rumen (9) and horse’s colon(7). The highest isolates activity of lignolytic, xylanolytic, and cellulolytic were reached by buffalo’scecum (7.64), horse's cecum (6.27), and buffalo’s colon (2.48). Meanwhile the highest enzymesproductivities were: buffalo’s cecum (0.0400 µmol), horse’s cecum (1.3912 µmol) and buffalo’s colon(0.1971 µmol). Based on morphologycal character and biochemical test, it could be concluded thatlignolytic from buffalo’s cecum, xylanolytic from horse’s cecum, and cellulolytic from buffalo’s colonwere the superior isolates and they were 99% analyzed as Enterococcus casseliflavus/gallinarumspecies.
Co-Authors A. Wahyudi E. Suryanto J. Jamhari L.M. Yusiati M. Muguruma M. Soejono Y. Erwanto Z. Bachruddin