Utilization of coffee skin fiber as potential source of reducing sugar by means on enzymatic hydrolysis
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Dec 31, 2018
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Coffee spent ground is a primary by-product obtained during soluble coffee processing and potential to be utilized as a high value product due to its protein content. The quite popular effort to utilize protein-contained material is to process it to hydrolysate which also possess antioxidant activity. This research was aimed to study the possibility of protein and antioxidative compound from coffee spent ground by means of enzymatic hydrolysis using crude papain enzymes. Crude papain was used in different concentration ranged from 2, 4 and 6% to incubate the coffee spent grounds for 2, 3, and 4 hours and then analyzed for its protein content and its antioxidant activity, whereas response surface methodology was employed to study the tendency of the effect of incubation time and enzymes concentration towards hydrolysis results. The result showed that the use of crude papain was effective to liberate the protein and antioxidant compound the coffee spent ground with its optimum condition utilized 6% of enzyme and 2 hours incubation time. At mentioned condition, it could extract up to 67.38% of the protein of the coffee spent ground and its hydrolysate possessed relatively high antioxidant activity.
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Febrianto, N. (2018). Utilization of coffee skin fiber as potential source of reducing sugar by means on enzymatic hydrolysis. Pelita Perkebunan (a Coffee and Cocoa Research Journal), 34(3), 166-174. https://doi.org/10.22302/iccri.jur.pelitaperkebunan.v34i3.285
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References
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Apiwatanapiwat, W, P. Vaithanomsat, P. Somkliang, & T. Malapant. (2009). Optimization of protein hydrolysate production process from jathropa curcas cake. WASET International Journal of Agricultural and Biosystem Engineering, 3, 250-253
BSN. (2014). SNI 3747-2013 Kakao Bubuk. Badan Standardisasi Nasional, Jakarta, Indonesia
Centenaro, G.S., M.S. Mellado, & C. Prentice-Hernandez. 2011. Antioxidant activity of protein hydrolysates of fsh and chicken bones. Advance Journal of Food Science and Technology, 3, 280-288.
Chapot-Chartier, M.P. & M.Y. Mistou. (2004). PepC aminopeptidase of lactic acid bacteria. In A.J. Barrett, N.D. Rawlings & J.F. Woessner (Eds). Handbook of Proteolytic Enzymes, p. 1202–1204, Elsevier, London.
Dudley, E.G. & J.L. Steele. (2004). Dipeptidase DA. In A.J. Barrett, N.D. Rawlings & J.F. Woessner (Eds). Handbook of Proteolytic Enzymes, p. 2052–2053, Elsevier, London.
Febrianto, N.A. (2013). Hidrolisat Protein asal Bungkil Kakao dan Ampas Kopi. Warta Pusat Penelitian Kopi dan Kakao Indonesia, 25(3), 20-23.
Foh, M.B.K., I. Amadou, B. Foh, M., M.T. Kamara & W. Xia. (2010). Functionality and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by the degree of hydrolysis. International Journal of Molecular Sciences, 11(4), 1851-1869.
Gallegos-Tintore, S., C.T. Fuentes, J.S. Feria, M. Alaiz, J.G. Calle, A.L.M. Ayala, L.C. Guerrero & J Vioque. (2011). Antioxidant and chelating activity of jatropa curcas l. protein hydrolysates. Journal of the Science of Food and Agriculture, 91(9), 1618-1624.
Graf, L., L. Szilagy. & I. Venekei. (2004). Chymotrypsin. In A.J. Barrett, N.D. Rawlings & J.F. Woessner (Eds). Handbook of Proteolytic Enzymes, p. 1495–1501, Elsevier, London.
Hamada, J.S. (2000). Characterization and functional properties of rice bran proteins modified by commercial exoproteases and endoproteases. Journal of Food Science, 65(2), 305-310.
Haslaniza, H., M.Y. Maskat, W.M.W. Aida, & s. Mamot. (2010). The effects of enzyme concentration, temperature and incubation time on nitrogen content and degree of hydrolysis of protein precipitate from cockle (Anadara granosa) meat wash water. International Food Research Journal, 17, 147-152.
Herpandi (2013). Enzymatic hydrolysis of tuna by ptoducts: physico-chemical characteristics, digestibility and antioxidative properties of the hydrolysate. Penang, Malaysia: Universiti Sains Malaysia, PhD thesis.
Herpandi, A. Rosma, W.A.W. Nadiah, N.A. Febrianto, & N. Huda. (2017). Optimization of enzymatic hydrolysis of skipjack tuna by-product using protamex: a response surface approach. Journal of Fundamental and Applied Sciences, 9(2S), 845-860.
Hoyle, N.T., & J.H. Merrit. (1994). Quality of fish protein hydrolysates from Herring (Clupea harengus). Journal of Food Science, 59, 76-79
Je J.Y., P.J. Park & S.K. Kim. (2005). Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Research International, 38, 45–50.
Je J.Y., Z.J. Qian, H.G. Byun & S.K. Kim. (2007). Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis. Process Biochemistry, 42, 840–846.
Jun, S.Y., P.J. Park, W. Jung & S.K. Kim. (2004). Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. European Food Research and Technology, 219(1), 20-26.
Kalantzakis G., G. Blekas, K. Pegklidou & D. Boskou. (2006). Stability and radical-scavenging activity of heated olive oil and other vegetable oils. European Journal of Lipid Science and Technology, 108, 329-335
Karamac, M., A Kosinka-Cagnazzo, & A. Kulcyk. (2016). Use of different proteases to obtain flaxseed protein hydrolysates with antioxidant activity. International Journal of Molecular Sciences, 17, 1-13
Ovissipour, M., A.A. Kenari, A. Motamedzadegan, B. Rasco & R.M. Nazari. (2011). Optimization of protein recovery during hydrolysis of yellowfin tuna (Thunnus albacares) visceral proteins. Journal of Aquatic Food Product Technology, 20(2), 148-159.
Pasupuleti, V. K. & S. Braun. (2010). State of the art manufacturing of protein hydrolysates. Protein Hydrolysates in Biotechnology, 11–32.
Rawlings, N. D., F.R. Morton & A.J. Barrett. (2007). An introduction to peptidases and the MEROPS database. In J. Polaina & A.P.MacCabe (Eds). Industrial Enzymes – Structure, Function and Applications, p. 161-179, Springer, Dordrecth, Netherlands
Sani, 2008. Penambahan Natrium Bisulfit pada Kualitas Enzim Papain dari Getah Pepaya Secara MCU. Unesa University Press, Surabaya, Indonesia
Shahidi F. & Y. Zhong. (2008). Bioactive peptides. Journal of American Organization of Analytical Chemistry International, 91(4), 914-931.
Simpsona, B.K., G. Nayeria, V. Yaylayana, & I.N.A. Ashieb. (1998). Enzymatic hydrolysis of shrimp meat. Food Chemistry, 1-2, 131-138
Sudarmadji S., B. Haryono & Suhardi. (1997). Prosedur Analisa untuk Bahan Makanan dan Pertanian. Liberty, Jogjakarta, Indonesia.
Tsuge, H., T. Nishimura, Y. Tada, T. Asao, D. Turk, V. Turk, & N. Katunuma, (1999). Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papainCLIK148 complex. Biochemical and Biophysical Research Communications, 266, 411-416.
Uhlig, H., (1998). Industrial Enzymes and their Applications. 1st Edn., John Wiley and Sons, New York.
Viera, G. H. F., A.M. Martin, S. Saker-Sampaiao, S. Omar, & C.F. Goncalves. (1995). Studies on the enzymatic hydrolysis of Brazilian lobster (Panulirus spp.) processing wastes. Journal Science Food Agricultural 69, 61–65.
Wu W.A., N.S. Hettiarachchy & M. Qi. (1998). Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. Journal of American Oil Chemist Society, 75(7), 845-850.
Zarei, M., A. Ebrahimpour, A. Abdul-Hamid, F. Anwar & N. Saari. (2012). Production of defatted palm kernel cake protein hydrolysate as a valuable source of natural antioxidants. International Journal of Molecular Sciences, 13, 8097-8111.
Zhang, M., T.H. Mu, Y.B. Wang & M.J. Sun. (2012). Evaluation of free radical-scavenging activities of sweet potato protein and its hydrolysates as affected by single and combination of enzyme systems. International Journal of Food Science and Technology, 47(4), 696-702
Apiwatanapiwat, W, P. Vaithanomsat, P. Somkliang, & T. Malapant. (2009). Optimization of protein hydrolysate production process from jathropa curcas cake. WASET International Journal of Agricultural and Biosystem Engineering, 3, 250-253
BSN. (2014). SNI 3747-2013 Kakao Bubuk. Badan Standardisasi Nasional, Jakarta, Indonesia
Centenaro, G.S., M.S. Mellado, & C. Prentice-Hernandez. 2011. Antioxidant activity of protein hydrolysates of fsh and chicken bones. Advance Journal of Food Science and Technology, 3, 280-288.
Chapot-Chartier, M.P. & M.Y. Mistou. (2004). PepC aminopeptidase of lactic acid bacteria. In A.J. Barrett, N.D. Rawlings & J.F. Woessner (Eds). Handbook of Proteolytic Enzymes, p. 1202–1204, Elsevier, London.
Dudley, E.G. & J.L. Steele. (2004). Dipeptidase DA. In A.J. Barrett, N.D. Rawlings & J.F. Woessner (Eds). Handbook of Proteolytic Enzymes, p. 2052–2053, Elsevier, London.
Febrianto, N.A. (2013). Hidrolisat Protein asal Bungkil Kakao dan Ampas Kopi. Warta Pusat Penelitian Kopi dan Kakao Indonesia, 25(3), 20-23.
Foh, M.B.K., I. Amadou, B. Foh, M., M.T. Kamara & W. Xia. (2010). Functionality and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by the degree of hydrolysis. International Journal of Molecular Sciences, 11(4), 1851-1869.
Gallegos-Tintore, S., C.T. Fuentes, J.S. Feria, M. Alaiz, J.G. Calle, A.L.M. Ayala, L.C. Guerrero & J Vioque. (2011). Antioxidant and chelating activity of jatropa curcas l. protein hydrolysates. Journal of the Science of Food and Agriculture, 91(9), 1618-1624.
Graf, L., L. Szilagy. & I. Venekei. (2004). Chymotrypsin. In A.J. Barrett, N.D. Rawlings & J.F. Woessner (Eds). Handbook of Proteolytic Enzymes, p. 1495–1501, Elsevier, London.
Hamada, J.S. (2000). Characterization and functional properties of rice bran proteins modified by commercial exoproteases and endoproteases. Journal of Food Science, 65(2), 305-310.
Haslaniza, H., M.Y. Maskat, W.M.W. Aida, & s. Mamot. (2010). The effects of enzyme concentration, temperature and incubation time on nitrogen content and degree of hydrolysis of protein precipitate from cockle (Anadara granosa) meat wash water. International Food Research Journal, 17, 147-152.
Herpandi (2013). Enzymatic hydrolysis of tuna by ptoducts: physico-chemical characteristics, digestibility and antioxidative properties of the hydrolysate. Penang, Malaysia: Universiti Sains Malaysia, PhD thesis.
Herpandi, A. Rosma, W.A.W. Nadiah, N.A. Febrianto, & N. Huda. (2017). Optimization of enzymatic hydrolysis of skipjack tuna by-product using protamex: a response surface approach. Journal of Fundamental and Applied Sciences, 9(2S), 845-860.
Hoyle, N.T., & J.H. Merrit. (1994). Quality of fish protein hydrolysates from Herring (Clupea harengus). Journal of Food Science, 59, 76-79
Je J.Y., P.J. Park & S.K. Kim. (2005). Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Research International, 38, 45–50.
Je J.Y., Z.J. Qian, H.G. Byun & S.K. Kim. (2007). Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis. Process Biochemistry, 42, 840–846.
Jun, S.Y., P.J. Park, W. Jung & S.K. Kim. (2004). Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. European Food Research and Technology, 219(1), 20-26.
Kalantzakis G., G. Blekas, K. Pegklidou & D. Boskou. (2006). Stability and radical-scavenging activity of heated olive oil and other vegetable oils. European Journal of Lipid Science and Technology, 108, 329-335
Karamac, M., A Kosinka-Cagnazzo, & A. Kulcyk. (2016). Use of different proteases to obtain flaxseed protein hydrolysates with antioxidant activity. International Journal of Molecular Sciences, 17, 1-13
Ovissipour, M., A.A. Kenari, A. Motamedzadegan, B. Rasco & R.M. Nazari. (2011). Optimization of protein recovery during hydrolysis of yellowfin tuna (Thunnus albacares) visceral proteins. Journal of Aquatic Food Product Technology, 20(2), 148-159.
Pasupuleti, V. K. & S. Braun. (2010). State of the art manufacturing of protein hydrolysates. Protein Hydrolysates in Biotechnology, 11–32.
Rawlings, N. D., F.R. Morton & A.J. Barrett. (2007). An introduction to peptidases and the MEROPS database. In J. Polaina & A.P.MacCabe (Eds). Industrial Enzymes – Structure, Function and Applications, p. 161-179, Springer, Dordrecth, Netherlands
Sani, 2008. Penambahan Natrium Bisulfit pada Kualitas Enzim Papain dari Getah Pepaya Secara MCU. Unesa University Press, Surabaya, Indonesia
Shahidi F. & Y. Zhong. (2008). Bioactive peptides. Journal of American Organization of Analytical Chemistry International, 91(4), 914-931.
Simpsona, B.K., G. Nayeria, V. Yaylayana, & I.N.A. Ashieb. (1998). Enzymatic hydrolysis of shrimp meat. Food Chemistry, 1-2, 131-138
Sudarmadji S., B. Haryono & Suhardi. (1997). Prosedur Analisa untuk Bahan Makanan dan Pertanian. Liberty, Jogjakarta, Indonesia.
Tsuge, H., T. Nishimura, Y. Tada, T. Asao, D. Turk, V. Turk, & N. Katunuma, (1999). Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papainCLIK148 complex. Biochemical and Biophysical Research Communications, 266, 411-416.
Uhlig, H., (1998). Industrial Enzymes and their Applications. 1st Edn., John Wiley and Sons, New York.
Viera, G. H. F., A.M. Martin, S. Saker-Sampaiao, S. Omar, & C.F. Goncalves. (1995). Studies on the enzymatic hydrolysis of Brazilian lobster (Panulirus spp.) processing wastes. Journal Science Food Agricultural 69, 61–65.
Wu W.A., N.S. Hettiarachchy & M. Qi. (1998). Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. Journal of American Oil Chemist Society, 75(7), 845-850.
Zarei, M., A. Ebrahimpour, A. Abdul-Hamid, F. Anwar & N. Saari. (2012). Production of defatted palm kernel cake protein hydrolysate as a valuable source of natural antioxidants. International Journal of Molecular Sciences, 13, 8097-8111.
Zhang, M., T.H. Mu, Y.B. Wang & M.J. Sun. (2012). Evaluation of free radical-scavenging activities of sweet potato protein and its hydrolysates as affected by single and combination of enzyme systems. International Journal of Food Science and Technology, 47(4), 696-702
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