Thumbnail
Access Restriction
Open

Researcher Vinoth, Kumar L.
Advisor Shanmugam, S. A.
Source KrishiKosh-Indian National Agricultural Research System
Content type Text
Educational Degree Master of Science (M.Sc.)
Publisher Fisheries College and Research Institute
File Format PDF
Language English
Subject Domain (in DDC) Technology ♦ Chemical engineering ♦ Food technology
Subject Keyword Fish Processing Technology ♦ Antimicrobial Activity of Biopeptides Extracted From Fish Protein Hydrolysate
Abstract Fish protein hydrolysates (FPH) were prepared from skin and muscle of fifteen fin fishes using commercial protease enzymes viz. alcalase, trypsin, pepsin and papain by optimizing different concentrations (0.25%, 0.50%, 0.75%, 1.00%, 1.25% and 1.50%) and reaction times (0, 15, 30, 45, 60, 75, 90, 105, 120, 135, 150, 165, 180, 195, 210, 225 and 240 min) with constant pH (7.0 for alcalase, 8.0 for trypsin, 2.0 for pepsin and 6.0 for papain) and temperature (500C for alcalase, 370C for trypsin, pepsin and papain). Based on the degree of hydrolysis (DH), the enzymatic hydrolysis process conditions were optimized. Generally, DH increased when the reaction times and enzyme concentrations increased. However, the rate of DH was faster during the initial phase of 60 min and thereafter the rate of DH was very low in the cases of trypsin, pepsin and papain treated samples, while the DH was stationary after 60 min with alcalase enzyme. The maximum DH of 82% was obtained within 60 min of reaction time with alcalase enzyme, followed by 51% DH with papain after 225 min, 50% DH with trypsin after 210 min and 29% DH with pepsin after 225 min at 1.00% concentration. Based on the results obtained, the process conditions optimized for enzymatic hydrolysis were: enzyme concentration 1.00%, reaction time 60 min, reaction temperature 500C and pH 7.0 for alcalase; enzyme concentration 1.00%, reaction time 60 min, reaction temperature 370C and pH 8.0 for trypsin; enzyme concentration 1.00%, reaction time 60 min, reaction temperature 370C and pH 2.0 for pepsin and enzyme concentrations 1.00%, reaction time 60 min, reaction temperature 370C and pH 6.0 for papain enzyme. Using the optimized process conditions, FPHs were prepared from the muscle and skin of 15 species of finfishes viz. Nemiptereus sp, Arius sp, Caranx sp, Plectorhinchus sp, Mugil cephalus, Hemiramphus sp, Scomberoides sp, Synaptura sp, Scomberomorus sp, Gerres sp, Lycenchelys scaurus, Epinephelus sp, Leiognathus sp, Rastrelliger kanagurta and Arothron stellatus and they were subjected to antimicrobial activity test against nine bacterial pathogens such as Escherichia coli, Enterobacter cloacae, Staphylococcus aureus, Aeromonas hydrophila, Vibrio cholerae, V. parahaemolyticus, Klebsiella pneumoniae, Pseudomonas aeruginosa and Listeria monocytogenes. None of the FPH prepared from fish muscle exhibited antimicrobial property, whereas FPH extracted from puffer fish skin using trypsin and alcalase showed some antimicrobial activity. Alcalase (1.00%) enzyme showed maximum antimicrobial activity against Staphylococcus aureus (9 mm), followed by Enterobacter cloacae (7 mm) and Escherichia coli (6 mm). Trypsin had maximum antimicrobial activity against Klebsiella pneumoniae (10 mm) followed by Enterobacter cloacae (6 mm) and Escherichia coli (5 mm). None of the biopeptides fractionated from trypsin derived fish skin protein hydrolysates showed antimicrobial activity against the selected bacterial pathogens. However, the biopeptide fraction (<30 KDa) derived from alcalase alone exhibited antimicrobial activity against Escherichia coli (2mm). Further research on sequencing of biopeptides having antimicrobial properties will be attempted.
Educational Use Research
Education Level UG and PG
Learning Resource Type Thesis
Publisher Place Tamil Nadu ♦ Thoothukudi
Owner Jeya, Shakila R. ♦ Karal, Marx K.
Size (in Bytes) 1.65 MB
Page Count 79