สมบัติบางส่วนของคอลลาเจนจากปลิงทะเลดำ (Holothuria leucospilota)
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บทคัดย่อ
การศึกษาบางสมบัติของคอลลาเจนจากปลิงทะเลดำ (Holothuria leucospilota) พบว่าผนังลำตัวของปลิงทะเลดำ 100 กรัม ของน้ำหนักเปียก สามารถสกัดคอลลาเจนหยาบได้ 10.95 กรัม ของน้ำหนักแห้ง และสามารถสกัด pepsin-solubilized collagen (PSC) จากคอลลาเจนหยาบได้ประสบผลสำเร็จ ปริมาณค่อนข้างสูง คือ ร้อยละ 66.46 การตรวจสอบโปรตีนด้วย SDS-PAGE พบว่าเป็นคอลลาเจน type I ประกอบด้วยสายเปปไทด์ a1 มีมวลโมเลกุลประมาณ 150 กิโลดาลตัน ประกอบด้วยกรดอะมิโนไกลซีน โปรลีน และไฮดรอกซีโปรลีน ร้อยละ 20.3, 8.8 และ 7.0 ของน้ำหนักแห้ง ตามลำดับ มีค่า transition temperature (Tmax) เท่ากับ 50.88 องศาเซลเซียส สามารถดูดกลืนแสงยูวีสูงสุดที่ความยาวคลื่น 235 นาโนเมตร และมีค่าการละลายสูงสุดที่พีเอช 1
คำสำคัญ : ปลิงทะเลดำ; คอลลาเจนที่ละลายด้วยเอนไซม์เปปซิน; การสกัด
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ประเภทบทความ
Biological Sciences
เอกสารอ้างอิง
[1] นรินทร์ ทาหอม และวรางคณา สมพงศ์, 2558, สมบัติของคอลลาเจนที่ละลายด้วยกรดจากหนังปลาสลาด, ว.วิทยาศาสตร์และเทคโนโลยี 23(2): 257-267.
[2] นริศ เจนวิริยะ, 2544, โรควัวบ้าเกิดจากสารโปรตีน, น.ใกล้หมอ 25(4): 74-75.
[3] Abedin, M.Z., Karim, A.A., Ahmed, F., Latiff, A.A., Gan, C.Y., Ghazali, F.C. and Sarker, M.Z.I., 2012. Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus), J. Sci. Food Agric. 93: 1083-1088.
[4] Adibzadeh, N., Aminzadeh, S., Jamili, S., Karkhane, A.A. and Farrokhi, N., 2014, Purification and characterization of pepsin-solubilized collagen from skin of sea cucumber Holothuria parva, Appl. Biochem. Biotechnol. 173: 143-154.
[5] Cui, F., Xue, C., Li, Z., Zhang, Y., Dong, P., Fu, X. and Gao, X., 2007, Characterization and subunit composition of collagen from the body wall of sea cucumber Stichopus japonicus, Food Chem. 100: 1120-1125.
[6] Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T. and Tanaka, M., 2005, Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus), Food Chem. 89: 363-372.
[7] Laemmli, U.K., 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227: 680-685.
[8] Li, G.Y., Fukunaga, S., Takenouchi, K. and Nakamura, F., 2005, Comparative study of the physiological properties of collagen, gelatin and collagen hydrolysate as cosmetic materials, Int. J. Cosmet. Sci. 27: 101-106.
[9] Li, H., Liu, B.L., Gao, L.Z. and Chen, H.L., 2004, Studies on bullfrog skin collagen, Food chem. 84: 65-69.
[10] Liu, Z., Oliveira, A.C.M. and Su, Y.C., 2010, Purification and characterization of pepsin-solubilized collagen from skin and connective tissue of giant red sea cucumber (Parastichopus californicus), J. Agric. Food Chem. 58: 1270-1274.
[11] Montero, P., Jimenez-Colmenero, F. and Borderias, J., 1991. Effect of pH and the presence of NaCl on some hydration properties of collagenous material from trout (Salmo irideus Gibb) muscle and skin, J. Sci. Food Agric. 54: 137-146.
[12] Myllyharju, J., 2005, Intracellular post-translational modifications of collagens, Curr. Top. Med. 247: 115-147.
[13] Park, S.Y., Lim, H.K., Lee, S., Hwang, H.C., Cho, S.K. and Cho, M., 2012, Pepsin-solubilised collagen (PSC) from Red Sea cucumber (Stichopus japonicus) regulates cell cycle and the fibronectin synthesis in HaCaT cell migration, Food Chem. 32: 487-492.
[14] Sato, K., Yoshinaka, R., Sato, M. and Shimizu, Y., 1987, Isolation of native acid-soluble collagen from fish muscle, Nippon Suisan Gakkaishi 53: 1431-1436.
[15] Senaratne, L.S., Park, P. and Kim, S., 2006, Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin, Biores. Technol. 97: 191-197.
[16] Siddiqui, Y. D., Arief, E.M., Yusoff, A., Suzina A.H. and Abdullah, S.Y., 2013, Isolation of pepsin-solubilized collagen (PSC) from crude collagen extracted from body wall of sea cucumber (Bohadschia spp), Int. J. Pharm. Pharmaceut. Sci. 5: 555-559.
[17] Swatschek, D., Schatton, W., Kellermann, J., Muller, W.E.G. and Kreuter, J., 2002, Marine sponge collagen: Isolation, characterization and effects on the skin parameters surface-pH, moisture and sebum, Eur. J. Pharmaceut. Biopharm. 53: 107-113.
[18] Tamimi, F., Kumarasami, B., Doillon, C., Gbureck, U., Le Nihouannen, D., Cabarcos, E.L. and Barralet, J.E., 2008, Brushite-collagen composite for bone regeneration, Acta Biomaterialia 4: 1315-1321.
[19] Trotter, J.A., Lyons-Levy, G., Thurmond, F.A. and Koobt, T.J., 1995, Covalent composition of collagen fibrils from the dermis of the sea cucumber, Cucumaria frondosa, a tissue with mutable mechanical properties, Comp. Biochem. Physiol. A. 112: 463-478.
[2] นริศ เจนวิริยะ, 2544, โรควัวบ้าเกิดจากสารโปรตีน, น.ใกล้หมอ 25(4): 74-75.
[3] Abedin, M.Z., Karim, A.A., Ahmed, F., Latiff, A.A., Gan, C.Y., Ghazali, F.C. and Sarker, M.Z.I., 2012. Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus), J. Sci. Food Agric. 93: 1083-1088.
[4] Adibzadeh, N., Aminzadeh, S., Jamili, S., Karkhane, A.A. and Farrokhi, N., 2014, Purification and characterization of pepsin-solubilized collagen from skin of sea cucumber Holothuria parva, Appl. Biochem. Biotechnol. 173: 143-154.
[5] Cui, F., Xue, C., Li, Z., Zhang, Y., Dong, P., Fu, X. and Gao, X., 2007, Characterization and subunit composition of collagen from the body wall of sea cucumber Stichopus japonicus, Food Chem. 100: 1120-1125.
[6] Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T. and Tanaka, M., 2005, Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus), Food Chem. 89: 363-372.
[7] Laemmli, U.K., 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227: 680-685.
[8] Li, G.Y., Fukunaga, S., Takenouchi, K. and Nakamura, F., 2005, Comparative study of the physiological properties of collagen, gelatin and collagen hydrolysate as cosmetic materials, Int. J. Cosmet. Sci. 27: 101-106.
[9] Li, H., Liu, B.L., Gao, L.Z. and Chen, H.L., 2004, Studies on bullfrog skin collagen, Food chem. 84: 65-69.
[10] Liu, Z., Oliveira, A.C.M. and Su, Y.C., 2010, Purification and characterization of pepsin-solubilized collagen from skin and connective tissue of giant red sea cucumber (Parastichopus californicus), J. Agric. Food Chem. 58: 1270-1274.
[11] Montero, P., Jimenez-Colmenero, F. and Borderias, J., 1991. Effect of pH and the presence of NaCl on some hydration properties of collagenous material from trout (Salmo irideus Gibb) muscle and skin, J. Sci. Food Agric. 54: 137-146.
[12] Myllyharju, J., 2005, Intracellular post-translational modifications of collagens, Curr. Top. Med. 247: 115-147.
[13] Park, S.Y., Lim, H.K., Lee, S., Hwang, H.C., Cho, S.K. and Cho, M., 2012, Pepsin-solubilised collagen (PSC) from Red Sea cucumber (Stichopus japonicus) regulates cell cycle and the fibronectin synthesis in HaCaT cell migration, Food Chem. 32: 487-492.
[14] Sato, K., Yoshinaka, R., Sato, M. and Shimizu, Y., 1987, Isolation of native acid-soluble collagen from fish muscle, Nippon Suisan Gakkaishi 53: 1431-1436.
[15] Senaratne, L.S., Park, P. and Kim, S., 2006, Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin, Biores. Technol. 97: 191-197.
[16] Siddiqui, Y. D., Arief, E.M., Yusoff, A., Suzina A.H. and Abdullah, S.Y., 2013, Isolation of pepsin-solubilized collagen (PSC) from crude collagen extracted from body wall of sea cucumber (Bohadschia spp), Int. J. Pharm. Pharmaceut. Sci. 5: 555-559.
[17] Swatschek, D., Schatton, W., Kellermann, J., Muller, W.E.G. and Kreuter, J., 2002, Marine sponge collagen: Isolation, characterization and effects on the skin parameters surface-pH, moisture and sebum, Eur. J. Pharmaceut. Biopharm. 53: 107-113.
[18] Tamimi, F., Kumarasami, B., Doillon, C., Gbureck, U., Le Nihouannen, D., Cabarcos, E.L. and Barralet, J.E., 2008, Brushite-collagen composite for bone regeneration, Acta Biomaterialia 4: 1315-1321.
[19] Trotter, J.A., Lyons-Levy, G., Thurmond, F.A. and Koobt, T.J., 1995, Covalent composition of collagen fibrils from the dermis of the sea cucumber, Cucumaria frondosa, a tissue with mutable mechanical properties, Comp. Biochem. Physiol. A. 112: 463-478.