Open AccessCellulase derived from Chryseobacterium indologenes LA4K isolated from Indonesian agar-agar industry solid waste
Author(s) -
Ifah Munifah,
Jamal Basmal,
Rinta Kusumawati,
Hari Eko Irianto
Publication year - 2020
Publication title -
iop conference series. earth and environmental science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.179
H-Index - 26
eISSN - 1755-1307
pISSN - 1755-1315
DOI - 10.1088/1755-1315/462/1/012007
Subject(s) - cellulase , agar , hydrolysis , chemistry , food science , enzyme , incubation , substrate (aquarium) , chromatography , enzyme assay , microbiology and biotechnology , nuclear chemistry , biochemistry , bacteria , biology , ecology , genetics
Hydrolysis process can be a challenging task to perform because the required enzymes are difficult to find and microbial culture is relatively expensive. However, the process can be made more economical by utilizing enzymes which can be produced using substrates derived from local materials. One example of such materials is the solid waste generated by industries involving agar-agar which is obtained from the red alga Gracilaria sp. Chryseobacterium indologenes LA4K is an indigenous bacterial variant which is isolated from agar-agar industry solid waste. The cellulolytic enzyme of C. indologenes LA4K was processed using a medium of 2.5% agar-agar industry solid waste which was incubated for six days and showed an activity of 0.3726 U/mL. Reaction incubation temperature exerted some influence on the activity of C. indologenes LA4K: the process produced the optimum activity of 0.3246 U/mL at the temperature of 40°C, while 30 minutes was determined as the optimum incubation period needed by both enzyme and substrate of C. indologenes LA4K to react. The enzyme entirely lost its activity when heated to the temperature of 80°C. The activity of LA4K cellulase increased with an addition of divalent ions (Mg 2+ , Ca 2+ , and Zn 2+ ) and monovalent ions (K + and Na + ). An addition of trivalent ion Fe 3+ to C. indologenes LA4K cellulase acted as an inhibitor to its activity. Addition of ethanol as an organic solvent to the supernatant crude enzyme caused the enzyme to become denatured, thus reducing the cellulase activity of its C. indologenes LA4K isolate to 85.47%. The presence of anionic detergent SDS in the crude cellulase of C. indologenes LA4K increased its activity to 105%. Addition of nonionic detergents Triton X-100 and Tween 80 to C. indologenes LA4K cellulase increased its activity to 130% and 110.9%, respectively.