Isolation and characterization of proteins from Sarcodia montagneana and their potential bioactivies

• Main Authors: Minguel, Jessica, 潔西卡
• Other Authors: Chang, Yu-Wei
• Format: Others
• Language: en_US
• Published: 2017
• Online Access: http://ndltd.ncl.edu.tw/handle/cbajay

碩士 === 國立臺灣海洋大學 === 食品科學系 === 105 === As a potential alternative protein source, Sarcodia montagneana, was subjected to protein extraction. The protein isolates (PI) were evaluated for their functional properties and potential bioactive peptides. The seaweed powder had a 14.11 ± 0.19% crude protein. The protein extraction was done in two solutions: (1) aqueous (Aq), with a higher yield (1.84 ± 2.02%) than with (2) alkaline (Alk), (0.53 ± 0.58%), having a protein content of 73.78 ± 1.46% and 91.63% ± 5.77%, respectively, and with no significant difference. At pH 12, both Aq and alk PIs attained the highest solubility with 29.70 ± 4.93% and 84.82 ± 4.61%, respectively. The water-holding capacity (WHC) of Aq PI (11.32 ± 0.17 ml H2O/ g PI) was significantly higher than the Alk PI (8.21 ± 0.60 ml H2O/g PI). The oil-holding capacities (OHC) of the PIs were 4.06 ± 0.76 ml oil/g PI and 4.32 ± 0.67 ml oil/g PI, respectively. The highest foam capacity was reached at pH 10 for Aq PI (43.54 ± 6.96%) and Alk PI (63.12 ± 12.98%). The most stable emulsion was formed with soybean oil for both PIs with Aq E1350= 65.69 ± 1.16% and Alk E1350= 59.05 ± 1.65%. Proteomic techniques were also carried out. The BIOPEP database was used to determine potential peptides with reported bioactivities of the identified proteins. The predictive results showed that S. montagneana have the highest occurrence of peptides as DPP IV inhibitors, with other high frequency bioactive peptides, ACE inhibitors, antioxidants, ion flow or stomach mucosal membrane activity regulators and glucose uptake or vasoactive substance release stimulants. With BIOPEP’s in silico hydrolysis, it showed that ficain, pepsin (pH > 2), proteinase K, papain and pancreatic elastase released greater numbers of bioactive peptides than other proteases. The results suggest the potential of S. montagneana PI as an inexpensive protein source to be incorporated into several value-added food products and other suitable applications.