Stability of Amylase Crude Powder from Aspergillus awamori KT-11 at Different Storage Temperatures

Urip Perwitasari, Ario Betha Juanssilfero, Ade Andriani, Ruth Melliawati, - Fahrurrozi, Ahmad Fathoni, - Sulat, Mukhammad Asy’ari, - Yopi

Abstract


Amylase is one kind of biotechnology product that has been used in many sector industries. Production of amylase powder from Aspergillus awamori KT-11 has been optimized successfully in the previous study. However, the stability of its activity, which is crucial in industrial application, has not yet been well studied. This study aimed to investigate the stability of amylase crude powder activity from A. awamori KT-11 at different storage temperatures. Amylase crude powder was stored at 4oC and 25oC. For the stability test, the crude powder with optimum storage temperature was diluted with phosphate buffer pH 4.8 and stored at 4oC, 25oC, and -20oC. The results showed that the activity of amylase crude powder was stable at 25 oC after nine months of storage with total activity of 2807 U/mL. On the other hand, the amylase extract liquid enzyme shows better activity when stored at 4 oC (with total activity 1000 U/mL after four-week storage time) than stored at temperatures 25oC or -20 oC. The findings also showed that crude amylase liquid extracts are not stored in a negative temperature environment. This is beneficial to enterprises because it lowers the cost of obtaining negative temperatures and saves energy.

Keywords


Enzyme stability; Aspergillus awamori KT-11; storage temperature; extract liquid enzyme.

Full Text:

PDF

References


R. A. Purnamasari, T. Ahamed, and R. Noguchi, “Land suitability assessment for cassava production in Indonesia using GIS, remote sensing and multi-criteria analysis,” Asia-Pacific J. Reg. Sci., vol. 3, no. 1, pp. 1–32, 2019, doi: 10.1007/s41685-018-0079-z.

E. O. Alamu, P. Ntawuruhunga, T. Chibwe, I. Mukuka, and M. Chiona, “Evaluation of cassava processing and utilization at household level in Zambia,” Food Secur., vol. 11, no. 1, pp. 141–150, 2019, doi: 10.1007/s12571-018-0875-3.

A. Edhirej, S. M. Sapuan, M. Jawaid, and N. I. Zahari, “Polyvinyl Alcohol-Modified Pithecellobium Clypearia Benth Herbal Residue FiberPolypropylene Composites,” Polym. Compos., vol. 37, no. 1, pp. 915–924, 2016, doi: 10.1002/pc.

S. Pradyawong, A. Juneja, M. Bilal Sadiq, A. Noomhorm, and V. Singh, “Comparison of cassava starch with corn as a feedstock for bioethanol production,” Energies, vol. 11, no. 12, pp. 1–11, 2018, doi: 10.3390/en11123476.

C. O. Ofuya and S. N. Obilor, “The suitability of fermented cassava peel as a poultry feedstuff,” Bioresour. Technol., vol. 44, no. 2, pp. 101–104, 1993, doi: 10.1016/0960-8524(93)90181-A.

U. Perwitasari, N. Nuryati, R. Melliawati, and Y. Yopi, “Glucoamylase Production by Aspergillus awamori KT-11 In Solid State Fermentation Using Cassava Peel as Substrate,” Ann. Bogor., vol. 21, no. 1, p. 21, 2018, doi: 10.14203/ann.bogor.2017.v21.n1.21-28.

A. Sani, F. A. Awe, and J. A. Akinyanju, “Amylase Synthesis in Aspergillus-Flavus and Aspergillus-Niger Grown on Cassava Peel,” J. Ind. Microbiol., vol. 10, no. 1, pp. 55–59, 1992.

K. M. Khalid-Bin-Ferdaus et al., “Commercial production of alpha amylase enzyme for potential use in the textile industries in Bangladesh,” Int. J. Biosci., vol. 13, no. 04, pp. 149–157, 2018, doi: 10.12692/ijb/13.4.149-157.

L. He et al., “Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization,” BMC Biotechnol., vol. 17, no. 1, pp. 1–13, 2017, doi: 10.1186/s12896-017-0343-8.

S. Uzuner and D. Cekmecelioglu, Enzymes in the Beverage Industry. Elsevier Inc., 2019.

R. Sindhu, P. Binod, and A. Pandey, “α-Amylases,” Curr. Dev. Biotechnol. Bioeng. Prod. Isol. Purif. Ind. Prod., pp. 3–24, 2016, doi: 10.1016/B978-0-444-63662-1.00001-4.

A. Sundarram and T. P. Krishna Murthy, “α-Amylase Production and Applications: A Review,” J. Appl. Environ. Microbiol., vol. 2, no. 4, pp. 166–175, 2014, doi: 10.12691/jaem-2-4-10.

J. M. Choi, S. S. Han, and H. S. Kim, “Industrial applications of enzyme biocatalysis: Current status and future aspects,” Biotechnol. Adv., vol. 33, no. 7, pp. 1443–1454, 2015, doi: 10.1016/j.biotechadv.2015.02.014.

M. J. Moehlenbrock and S. D. Minteer, Introduction to the Field of Enzyme Immobilization and Stabilization Method and Protocols, 2nd ed., vol. 1504. New York, 2017.

T. Jiang et al., “Characterization of a thermostable raw-starch hydrolyzing α-amylase from deep-sea thermophile Geobacillus sp.,” Protein Expr. Purif., vol. 114, pp. 15–22, 2015, doi: 10.1016/j.pep.2015.06.002.

M. Somogyi, “Notes on Sugar Determination,” J. Biol. Chem., pp. 19–24, 1952.

A. B. Juanssilfero et al., “Effect of inoculum size on single-cell oil production from glucose and xylose using oleaginous yeast Lipomyces starkeyi Effect of inoculum size on single-cell oil production from glucose and xylose using oleaginous yeast Lipomyces starkeyi,” J. Biosci. Bioeng., vol. 125, no. 6, pp. 695–702, 2018, doi: 10.1016/j.jbiosc.2017.12.020.

U. Hölker, M. Höfer, and J. Lenz, “Biotechnological advantages of laboratory-scale solid-state fermentation with fungi,” Appl. Microbiol. Biotechnol., vol. 64, no. 2, pp. 175–186, 2004, doi: 10.1007/s00253-003-1504-3.

C. Valls, C. Rojas, G. Pujadas, S. Garcia-Vallve, and M. Mulero, “Characterization of the activity and stability of amylase from saliva and detergent: Laboratory practicals for studying the activity and stability of amylase from saliva and various commercial detergents,” Biochem. Mol. Biol. Educ., vol. 40, no. 4, pp. 254–265, 2012, doi: 10.1002/bmb.20612.

G. de S. Moura et al., “Stability of enzyme complex solid-state fermentation subjected to the processing of pelleted diet and storage time at different temperatures,” Rev. Bras. Zootec., vol. 45, no. 12, pp. 731–736, 2016, doi: 10.1590/S1806-92902016001200001.

A. Sharma et al., “Potential of in situ SSF laccase produced from Ganoderma lucidum RCK 2011 in biobleaching of paper pulp,” Bioprocess Biosyst. Eng., vol. 42, no. 3, pp. 367–377, 2019, doi: 10.1007/s00449-018-2041-x.

N. Chondrogianni et al., “Protein damage, repair and proteolysis,” Mol. Aspects Med., vol. 35, no. 1, pp. 1–71, 2014, doi: 10.1016/j.mam.2012.09.001.

Q. S. Xu, Y. S. Yan, and J. X. Feng, “Efficient hydrolysis of raw starch and ethanol fermentation: a novel raw starch-digesting glucoamylase from Penicillium oxalicum,” Biotechnol. Biofuels, vol. 9, no. 1, pp. 1–18, 2016, doi: 10.1186/s13068-016-0636-5.

H. Han et al., “Insight on the changes of cassava and potato starch granules during gelatinization,” Int. J. Biol. Macromol., vol. 126, pp. 37–43, 2019, doi: 10.1016/j.ijbiomac.2018.12.201.

L. R. F. Souto, M. Caliari, M. S. Soares Júnior, F. A. Fiorda, and M. C. Garcia, “Utilization of residue from cassava starch processing for production of fermentable sugar by enzymatic hydrolysis,” Food Sci. Technol., vol. 37, no. 1, pp. 19–24, 2017, doi: 10.1590/1678-457X.0023.

W. C. Lam, D. Pleissner, and C. S. K. Lin, “Production of fungal glucoamylase for glucose production from food waste.,” Biomolecules, vol. 3, no. 3, pp. 651–61, 2013, doi: 10.3390/biom3030651.

R. S. Prakasham, C. Subba Rao, R. Sreenivas Rao, and P. N. Sarma, “Enhancement of acid amylase production by an isolated Aspergillus awamori,” J. Appl. Microbiol., vol. 102, no. 1, pp. 204–211, 2007, doi: 10.1111/j.1365-2672.2006.03058.x.

T. Matsubara et al., “Degradation of raw starch granules by α-amylase purified from culture of Aspergillus awamori KT-11,” J. Biochem. Mol. Bol., vol. 37, no. 4, pp. 422–428, 2004, doi: 10.5483/BMBRep.2004.37.4.422.




DOI: http://dx.doi.org/10.18517/ijaseit.12.1.14595

Refbacks

  • There are currently no refbacks.



Published by INSIGHT - Indonesian Society for Knowledge and Human Development