In cheese making industry, plant enzymes are used to produce cheese. In Ouest Africa, they produced the cheese “waragashi” with the mix milk and the plant Calotropis procera. The objective of our study is to assess ability to coagulate milk of the latex from news plants Plumeria alba and Plumeria rubra. If the two plants can supplied Calotropis procera in cheese making. For the results, we observed that the latex of Plumeria alba and Plumeria rubra are richer in proteins and mineral elements than the latex of Calotropis procera. It appears that the milk clotting and proteolytic activities of the latex of Plumeria alba and Plumeria rubra reached their optimum at 75°C while those of Calotropis procera reached the optimum at 55°C but remained active above 60 and 70°C. The Proteolytic Activity of the latex of C. procera and the two species of Plumeria was maximal at concentrations of 10% and 20% in the reaction medium, respectively. Polyacrylamide gel electrophoresis revealed that Plumeria alba latex had proteins with molecular weights of 10 and 25 kDa while the molecular weights Plumeria rubra latex proteins were 10, 25, 45kDa. The MCA/ PA ratio of Calotropis procera, Plumeria alba and Plumeria rubra was 1142.86; 810.81 and 576.92 respectively. These two Plumeria latex could validly replace C. procera latex in the production of cheese.
| Published in | American Journal of Chemical Engineering (Volume 9, Issue 3) |
| DOI | 10.11648/j.ajche.20210903.11 |
| Page(s) | 47-52 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2021. Published by Science Publishing Group |
Plumeria, Latex, Enzymatic Activity, Wagashi
| [1] | Harboe M, Broe ML, Qvist KB, Law BA, Tamime AY ( eds). Technology of cheese making Wiley Blackwell, London. (2010). |
| [2] | Beka R, Guiama V, Delmont A, Donn P, Slomianny M, Libouga D. Glycosyl part identified within Balanites aegyptiaca fruit protease, International Journal of biological Macromolécules. International Journal of biological Macromolécules. (2011); 49 (3) 397–401. |
| [3] | Adetunji VO, Salawu OT. West African soft cheese "wara" processed with Calotropis procera and Carica papaya: A comparative assessment of nutritional values. African Journal of Biotechnology. (2008); 7, 3660-3662. |
| [4] | Egounlety M, Edema M., Yehouessi B, Ahouansou M. Production et qualité du Waragashi peuhl en République du Bénin. Rapport de Recherche, DNSA / FSA / UNB. (1994); p 30 – 33. |
| [5] | Osseyi EG, Lamboni C R. Propriétés physico-chimiques et réactivité comparées des agents coagulants vegetaux dans la fabrication du fromage local frais "wagasi". J. Rech. Sci. Univ. Lomé (Togo). (2005); série A, 7 (1): 69-74. |
| [6] | Macalood JS, Vicente HJ, Boniao RD, Gorospe JG, Roa EC. Chemical Analysis of Carica papaya L. Crude Latex. American Journal of Plant Sciences. (2013); 1941–1948. |
| [7] | AOAC. Official Methods of Analysis, Association of Official Analytical Chemist Inc: Virginia, USA. (1990). |
| [8] | Darné G, Madero-Tamargo J. Mise au point d’une méthode d’extraction des lipides solubles totaux, des glucides solubles totaux et des composés phénoliques solubles totaux des organes de la vigne. Laboratoire de Physiologie Végétale et Ampélogie de l’Université de Bordeaux I, France, (1979); 221-228. |
| [9] | Oseni OA, and Ekperigin MM: Partial characterization of proteolytic and milk clotting enzymes in sodom apple Calotropis procera (Ait) R. Br. (Asclepiadaceaae) plant. Biology American journal of Biochemistry and Molecular (2013); 3 (2): 256-263. |
| [10] | Arima K, Iwasaki Yu: Milk clotting enzyme from Mucor pusillus var. Methods in enzymology. (1970); p 446-459. |
| [11] | Ladd JN, and et Butter JHA: Short-term assays of soil proteolytic enzyme activities using proteins and dipeptide derivatives as substrates. Soil Biol Biochemistry. (1972); 4, 19-30. |
| [12] | Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. (1970); 227–680. |
| [13] | Lynn KR, Clevette-Radford. Biochemical properties of latices from the Euphorbiaceae, Phytochemistry. (1987); 26, 939–944. |
| [14] | Moussaoui MEl, Nijs C, Paul R, Wintjens J, Vincentelli M, Azarkan, Looze Y. Revisiting the enzymes stored in the laticifers of Carica papaya in the context of their possible participation in the plant defence mechanism, Molécular. Life Science. (2001); 58 p 556–570. |
| [15] | Jeana S, Macalood HJ, Vicente RD, Boniao JG, Gorospe ECR. Chemical Analysis of Carica papaya L. Crude Latex. American Journal of Plant Sciences. (2013); 1941–1948. |
| [16] | Milaiti M, Traore AS, Moletta R. Détermination de la composition physico-chimique des feuilles de Calotropis procera provenant de Ouagadougou (Burkina Faso) et de N'Djaména (Tchad). (2003); 02, 73-78. |
| [17] | Temegne CN.; Ngome AF, Fotso KA. Influence de la composition chimique du sol sur la teneur en éléments nutritifs et le rendement du manioc (Manihot esculenta Crantz, Euphorbiaceae) dans deux régions agro ecologiques du Caméroun. International journal of biological and Chemical Sciences. (2015); 9 (6): 2776-2788. |
| [18] | Mazou M. Caractérisation et application des latex de plantes dans la catalyse de la transesterification éthanolique d’huile végétale dans la production du biodiesel. (2017). |
| [19] | Silvestre M, Carréira R, Sylvia M, Corgosinho F, Monteiro M, Morais H. Effect of pH and temperature on enzymatic activity of extract from pineapple peel. Food and bioprocess technology. (2012); 5.5, 1824–1831. |
| [20] | Chanda I, Sanat KB, Sadhan KD, Smriti RCD. A protease Isolated from latex of Plumeria rubra Linn (Aponyaceae): purification and characterization. Journal of Chemical and Pharmaceutical Research. (2011); 8 (5): 354-35. |
| [21] | Lo peiro AR, Puglisi IG. Characterization of “Lettucine” a serine like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting. Journal of agriculture and Food Chemistry (2002); 50, 2439- 2443. |
| [22] | Asakura T, Watanabe H, Abe K, and Arai S. Oryzasin as an aspartic proteinase occuring in rice seeds. Journal of Agricultural and Food Chemistry. (1997); 45, 1070-1075. |
| [23] | Rapaso S, Domingos A. Purification and characterization milk clotting aspartic proteinases from Centaurea calcitrapa cell suspension cultures. Process Biochemistry. (2008); 43, 139-144. |
| [24] | Dele R, Narinder S, Per E, Saris. The characterization and application of Calotropis procera, a coagulant in Nigerian Wara cheese. International journal of Food Science and Technology. (2007); 42 220-223. |
| [25] | Chitipinityol S, Crabbe MJC. Chymosin and aspartic proteinases. Food Chemistry. (1998); 61 395-418. |
| [26] | Chazarra S, Sidrach L, Lopez JN. Characterization of the milk-clotting properties of extracts from artichoke (Cynara scolymus, L.) flowers. International Dairy Journal. (2007); 17. 1393-1400. |
| [27] | Corrrons MA, Bertucci JI, Liggier CS, Lopz I, Bruno M. A. Milk clotting activity and production of bioactive peptides from whey using Maclura pomifera proteases. Food Science and Technology. (2012); 47, 103-109. |
| [28] | Mukundan MK, Gopakumar K, Nair MR. Purification of a lipase from the hepato pancreas of oil sardine (Sardinella longiceps Linnaeus) and its characteristics and properties. Journal of the Science of Food and Agriculture. (1985); 191–203. |
| [29] | Cambon E: Plantes laticifères. Mise en évidence et applications des activités lipasiques de Carica pentagona et Plumeria rubra. Universite montpellier II sciences et techniques du langue doc. École Doctorale: Sciences des procédés — Sciences des aliments, (2008); 154 pp. |
| [30] | Su H, Huang M, Wang H. Characterization of ginger proteases and their potantial as a rennin replacement. Journal of the Science of Food and Agriculture. (2009); vol 89; 1178-1185. |
| [31] | Mazorra-Manzano MA, Perea-Gutiérrez TC, Lugo-Sánchez ME, Ramirez-Suarez JC, Torres-Llanez MJ, González-Córdova AF, Vallejo-Cordoba B: Comparison of the milk-clotting properties of three plant extracts. Food Chemistry, (2013); 1902–1907. |
APA Style
Ibidjokè Rachidatou Bankole, Seid Ali Mahamat, Mouaïmine Mazou, Sênan Christa Marie Josephine Lokossou, Fidèle Paul Tchobo. (2021). Cheese-making Ability of Plumeria alba and Plumeria rubra Latex: Milk Clotting and Proteolytic Activities. American Journal of Chemical Engineering, 9(3), 47-52. https://doi.org/10.11648/j.ajche.20210903.11
ACS Style
Ibidjokè Rachidatou Bankole; Seid Ali Mahamat; Mouaïmine Mazou; Sênan Christa Marie Josephine Lokossou; Fidèle Paul Tchobo. Cheese-making Ability of Plumeria alba and Plumeria rubra Latex: Milk Clotting and Proteolytic Activities. Am. J. Chem. Eng. 2021, 9(3), 47-52. doi: 10.11648/j.ajche.20210903.11
AMA Style
Ibidjokè Rachidatou Bankole, Seid Ali Mahamat, Mouaïmine Mazou, Sênan Christa Marie Josephine Lokossou, Fidèle Paul Tchobo. Cheese-making Ability of Plumeria alba and Plumeria rubra Latex: Milk Clotting and Proteolytic Activities. Am J Chem Eng. 2021;9(3):47-52. doi: 10.11648/j.ajche.20210903.11
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Download@article{10.11648/j.ajche.20210903.11,
author = {Ibidjokè Rachidatou Bankole and Seid Ali Mahamat and Mouaïmine Mazou and Sênan Christa Marie Josephine Lokossou and Fidèle Paul Tchobo},
title = {Cheese-making Ability of Plumeria alba and Plumeria rubra Latex: Milk Clotting and Proteolytic Activities},
journal = {American Journal of Chemical Engineering},
volume = {9},
number = {3},
pages = {47-52},
doi = {10.11648/j.ajche.20210903.11},
url = {https://doi.org/10.11648/j.ajche.20210903.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajche.20210903.11},
abstract = {In cheese making industry, plant enzymes are used to produce cheese. In Ouest Africa, they produced the cheese “waragashi” with the mix milk and the plant Calotropis procera. The objective of our study is to assess ability to coagulate milk of the latex from news plants Plumeria alba and Plumeria rubra. If the two plants can supplied Calotropis procera in cheese making. For the results, we observed that the latex of Plumeria alba and Plumeria rubra are richer in proteins and mineral elements than the latex of Calotropis procera. It appears that the milk clotting and proteolytic activities of the latex of Plumeria alba and Plumeria rubra reached their optimum at 75°C while those of Calotropis procera reached the optimum at 55°C but remained active above 60 and 70°C. The Proteolytic Activity of the latex of C. procera and the two species of Plumeria was maximal at concentrations of 10% and 20% in the reaction medium, respectively. Polyacrylamide gel electrophoresis revealed that Plumeria alba latex had proteins with molecular weights of 10 and 25 kDa while the molecular weights Plumeria rubra latex proteins were 10, 25, 45kDa. The MCA/ PA ratio of Calotropis procera, Plumeria alba and Plumeria rubra was 1142.86; 810.81 and 576.92 respectively. These two Plumeria latex could validly replace C. procera latex in the production of cheese.},
year = {2021}
}
TY - JOUR T1 - Cheese-making Ability of Plumeria alba and Plumeria rubra Latex: Milk Clotting and Proteolytic Activities AU - Ibidjokè Rachidatou Bankole AU - Seid Ali Mahamat AU - Mouaïmine Mazou AU - Sênan Christa Marie Josephine Lokossou AU - Fidèle Paul Tchobo Y1 - 2021/06/15 PY - 2021 N1 - https://doi.org/10.11648/j.ajche.20210903.11 DO - 10.11648/j.ajche.20210903.11 T2 - American Journal of Chemical Engineering JF - American Journal of Chemical Engineering JO - American Journal of Chemical Engineering SP - 47 EP - 52 PB - Science Publishing Group SN - 2330-8613 UR - https://doi.org/10.11648/j.ajche.20210903.11 AB - In cheese making industry, plant enzymes are used to produce cheese. In Ouest Africa, they produced the cheese “waragashi” with the mix milk and the plant Calotropis procera. The objective of our study is to assess ability to coagulate milk of the latex from news plants Plumeria alba and Plumeria rubra. If the two plants can supplied Calotropis procera in cheese making. For the results, we observed that the latex of Plumeria alba and Plumeria rubra are richer in proteins and mineral elements than the latex of Calotropis procera. It appears that the milk clotting and proteolytic activities of the latex of Plumeria alba and Plumeria rubra reached their optimum at 75°C while those of Calotropis procera reached the optimum at 55°C but remained active above 60 and 70°C. The Proteolytic Activity of the latex of C. procera and the two species of Plumeria was maximal at concentrations of 10% and 20% in the reaction medium, respectively. Polyacrylamide gel electrophoresis revealed that Plumeria alba latex had proteins with molecular weights of 10 and 25 kDa while the molecular weights Plumeria rubra latex proteins were 10, 25, 45kDa. The MCA/ PA ratio of Calotropis procera, Plumeria alba and Plumeria rubra was 1142.86; 810.81 and 576.92 respectively. These two Plumeria latex could validly replace C. procera latex in the production of cheese. VL - 9 IS - 3 ER -
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