ARTIKEL REVIEW : STUDY α-AMILASE DARI MIKROBA SERTA PEMANFAATANYA DALAM PEMBUATAN MALTODEKSTRIN

Muhammad Alif Aziz Algofar, Hurryatul Fikri Rosmansyah, Ira Adiyati Rum, Soni Muhsinin, Fenti Fatmawati

Abstract


Amilase adalah hidrolase penting yang telah digunakan secara luas selama beberapa dekade. Enzim ini secara acak memotong ikatan glikosidik internal dalam molekul pati untuk menghidrolisisnya dan menghasilkan gula. Di antara amilase, α-amilase memiliki permintaan terbesar karena berbagai aplikasinya di bidang industri. Ketika konsumen menjadi lebih sadar akan masalah lingkungan, industri menemukan bahwa enzim dapat menggantikan katalis kimia lainnya. α-amilase dapat diproduksi dari tumbuhan atau sumber mikroba. Karena keuntungan yang diberikan oleh produksi mikroba, α-amilase dari mikroorganisme telah menjadi fokus perhatian dan lebih disukai daripada sumber produksi lainnya. Sifatnya yang ada di mana-mana, produksi yang mudah, dan berbagai aplikasi menjadikan α-amilase sebagai enzim yang penting bagi industri. Tujuan review ini adalah untuk memberikan informasi mengenai pengaplikasian enzim α-amilase yang berasal dari mikroba yaitu bakteri dan yeast serta pemanfaatannya dalam industri farmasi terutama dalam pembuatan maltodekstrin.

Kata kunci: α-Amilase ; Mikroba ; Maltodekstrin

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References


P. M. de Souza and P. de O. e Magalhães, “Application of microbial α-amylase in industry - a review,” Brazilian J. Microbiol., vol. 41, no. 4, pp. 850–861, 2010, doi: 10.1590/s1517-83822010000400004.

S. Pudjiraharti, S. Pudjiraharti, L. Z. Udin, and A. T. Karossi, “PRODUKSI ALFA-AMILASE OLEH ASPERGILLUS ORYZAE DALAM MEDIA PATI SAGU (Metroxylon sp.),” J. Kim. Terap. Indones. (Indonesian J. Appl. Chem., vol. 7, no. 1–2, pp. 1–2, 2017, [Online]. Available: https://inajac.lipi.go.id/index.php/InaJAC/article/view/221.

Ariandi, “Pengenalan Enzim Amilase (Alpha-Amylase) dan Reaksi Enzimatisnya Menghidrolisis Amilosa Pati Menjadi Glukosa,” J. Din., vol. 07, no. 1, pp. 74–82, 2016.

H. Rafsen, “OPTIMASI PRODUKSI DAN KARAKTERISASI ENZIM α -AMILASE DARI ISOLAT BAKTERI TERMOFIL Bacillus sp RSSII,” p. 71, 2018.

A. Sundarram and T. P. K. 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.

T. M. Silva et al., “Purification, partial characterization, and covalent immobilization–stabilization of an extracellular α-amylase from Aspergillus niveus,” Folia Microbiol. (Praha)., vol. 58, no. 6, pp. 495–502, 2013, doi: 10.1007/s12223-013-0230-1.

Tae Un Kim, Bu Gum Gu, Jae Yeon Jeong, Si Myung Byun, and Yong Chul Shin, “Purification and characterization of a maltotetraose-forming alkaline α- amylase from an alkalophilic Bacillus strain, GM8901,” Appl. Environ. Microbiol., vol. 61, no. 8, pp. 3105–3112, 1995, doi: 10.1128/aem.61.8.3105-3112.1995.

T. Hayashi, T. Akiba, and K. Horikoshi, “Production and Purification of New Maltohexaose-forming Amylases from Alkalophilic Bacillus sp. H-167,” Agric. Biol. Chem., vol. 52, no. 2, pp. 443–448, 1988, doi: 10.1271/bbb1961.52.443.

B. Khemakhem, M. Ben Ali, N. Aghajari, M. Juy, R. Haser, and S. Bejar, “Engineering of the α-amylase from geobacillus stearothermophilus US100 for detergent incorporation,” Biotechnol. Bioeng., vol. 102, no. 2, pp. 380–389, 2009, doi: 10.1002/bit.22083.

K. Memiliki, “Artikel Penelitian Pemurnian dan Karakterisasi Novel α- Amilase dari Bacillus subtilis,” vol. 12, no. 1, pp. 255–261, 2011.

B. Mohamed Babiker, M. Abd Elmahamoud Ahmed, and H. Ibrahim, “Isolation &Identification of Catalase Producing Bacillus spp: A Comparative Study,” Int. J. Adv. Res., vol. 4, no. 2, pp. 1206–1211, 2016, [Online]. Available: http://www.journalijar.com.

E. Demİrkan and M. Basil, “Produksi , pemurnian , dan karakterisasi α-amilase oleh Bacillus subtilis dan turunan mutannya,” vol. 35, pp. 705–712, 2011.

J. K. Roy, A. K. Manhar, D. Nath, M. Mandal, and A. K. Mukherjee, “Cloning and extracellular expression of a raw starch digesting α-amylase (Blamy-I) and its application in bioethanol production from a non-conventional source of starch,” J. Basic Microbiol., vol. 55, no. 11, pp. 1287–1298, 2015, doi: 10.1002/jobm.201400949.

S. Agüloǧlu Fincan, B. Enez, S. Özdemir, and F. Matpan Bekler, “Purification and characterization of thermostable α-amylase from thermophilic Anoxybacillus flavithermus,” Carbohydr. Polym., vol. 102, no. 1, pp. 144–150, 2014, doi: 10.1016/j.carbpol.2013.10.048.

R. Du et al., “Purification and characterization of novel thermostable and Ca-independent α-amylase produced by Bacillus amyloliquefaciens BH072,” Int. J. Biol. Macromol., vol. 115, no. 2017, pp. 1151–1156, 2018, doi: 10.1016/j.ijbiomac.2018.05.004.

N. Annamalai, R. Thavasi, S. Vijayalakshmi, and T. Balasubramanian, “Extraction, Purification and Characterization of Thermostable, Alkaline Tolerant α-Amylase from Bacillus cereus,” Indian J. Microbiol., vol. 51, no. 4, pp. 424–429, 2011, doi: 10.1007/s12088-011-0160-z.

O. K. Achi and A. N. U. Nijoku-Obi, “Production of a raw starch saccharifying amylase by Bacillus alvei grown on different agricultural substrates,” World J. Microbiol. Biotechnol., vol. 8, no. 2, pp. 206–207, 1992, doi: 10.1007/BF01195849.

F. G. Winarno, Enzim Pangan. Jakarta: PT. Gramedia Pustaka Utama, 1995.

Maiti and Bidinger, “‘Digital Repository Universitas Jember Digital Repository Universitas Jember,’” J. Chem. Inf. Model., vol. 53, no. 9, pp. 1689–1699, 1981.

N. S. Wang, “Experiment no. 5: Starch Hydrolysis by Amylase,” Univ. Maryl. Dep. Chem. Biomol. Eng., 2009.

“From Rabbit Livers With Cold Trichloroacetic,” vol. 71, pp. 405–417, 1965.

M. Sahnoun, S. Bejar, A. Sayari, M. A. Triki, M. Kriaa, and R. Kammoun, “Production, purification and characterization of two α-amylase isoforms from a newly isolated Aspergillus Oryzae strain S2,” Process Biochem., vol. 47, no. 1, pp. 18–25, 2012, doi: 10.1016/j.procbio.2011.09.016.

D. Oleh and S. Koswara, “Teknologi modifikasi pati,” 2009.

A. A. Maulani, A. Firmansyah, and A.Zainuddin, “Pembuatan maltodekstrin dari pati ubi jalar ( ipomoea batatas. poir) sebagai bahan tambahan sediaan farmasi,” Jstfi, vol. 1, no. 1, pp. 32–37, 2012.

T. Cerna, S. Pangan, and H. Herawati, “Potensi Pengembangan Produk Pati Tahan Cerna sebagai Pangan Fungsional,” J. Penelit. dan Pengemb. Pertan., vol. 30, no. 1, pp. 31–39, 2016, doi: 10.21082/jp3.v30n1.2011.p31-39.

P. Bernfeld, “Amylases, alpha and beta,” Methods Enzymol. I, vol. I, no. 540, pp. 149–158, 1955.

O. H. Lowry, N. J. Roserbrough, A. L. Farr, and N. J. Randall, “Estimation of total protein,” J. Biol. Chem., vol. 193, p. 265, 1951.

U. K. LAEMMLI, “Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970, doi: 10.1038/227680a0.

S. MITSUNAGA, O. KAWAKAMI, T. NUMATA, J. YAMAGUCHI, K. FUKUI, and T. MITSUI, “Polymorphism in Rice Amylases at an Early Stage of Seed Germination,” Biosci. Biotechnol. Biochem., vol. 65, no. 3, pp. 662–665, 2001, doi: 10.1271/bbb.65.662.

F. Xie et al., “Purification and characterization of a novel α-amylase from a newly isolated Bacillus methylotrophicus strain P11-2,” Process Biochem., vol. 49, no. 1, pp. 47–53, 2014, doi: 10.1016/j.procbio.2013.09.025.

S. Bano, S. A. U. Qader, A. Aman, M. N. Syed, and A. Azhar, “Purification and characterization of novel α-amylase from bacillus subtilis KIBGE HAS,” AAPS PharmSciTech, vol. 12, no. 1, pp. 255–261, 2011, doi: 10.1208/s12249-011-9586-1.

Y. H. Liu, F. P. Lu, Y. Li, J. L. Wang, and C. Gao, “Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations,” Appl. Microbiol. Biotechnol., vol. 80, no. 5, pp. 795–803, 2008, doi: 10.1007/s00253-008-1580-5.

H. Lee et al., “Artikel Karakterisasi dan Penerapan BiLA , Psikrofilik # -Amylase dari Bifidobacterium longum,” 2016.

G. Aguilar, J. Morlon-Guyot, B. Trejo-Aguilar, and J. P. Guyot, “Purification and characterization of an extracellular α-amylase produced by Lactobacillus manihotivorans LMG 18010(T), an amylolytic lactic acid bacterium,” Enzyme Microb. Technol., vol. 27, no. 6, pp. 406–413, 2000, doi: 10.1016/S0141-0229(00)00230-1.

A. Asoodeh, J. K. Chamani, and M. Lagzian, “A novel thermostable, acidophilic α-amylase from a new thermophilic ‘Bacillus sp. Ferdowsicous’ isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization,” Int. J. Biol. Macromol., vol. 46, no. 3, pp. 289–297, 2010, doi: 10.1016/j.ijbiomac.2010.01.013.

N. Hmidet, H. Maalej, A. Haddar, and M. Nasri, “A novel α-Amylase from Bacillus mojavensis A21: Purification and biochemical characterization,” Appl. Biochem. Biotechnol., vol. 162, no. 4, pp. 1018–1030, 2010, doi: 10.1007/s12010-009-8902-7.

S. K. Sudan, N. Kumar, I. Kaur, and G. Sahni, “Production, purification and characterization of raw starch hydrolyzing thermostable acidic α-amylase from hot springs, India,” Int. J. Biol. Macromol., vol. 117, pp. 831–839, 2018, doi: 10.1016/j.ijbiomac.2018.05.231.

N. Mollania, K. Khajeh, S. Hosseinkhani, and B. Dabirmanesh, “Purification and characterization of a thermostable phytate resistant α-amylase from Geobacillus sp. LH8,” Int. J. Biol. Macromol., vol. 46, no. 1, pp. 27–36, 2010, doi: 10.1016/j.ijbiomac.2009.10.010.

S. Erdal and M. Taskin, “Production of α-amylase by Penicillium expansum MT-1 in solid-state fermentation using waste loquat (Eriobotrya japonica Lindley) kernels as substrate,” Rom. Biotechnol. Lett., vol. 15, no. 3, pp. 5342–5350, 2010.

D. P. Sari, “ISOLASI, PURIFIKASI DAN KARAKTERISASI α-AMILASE DARI Saccharomyces cerevisiae FNCC 3012,” Chem Info J., vol. 1, no. 1, pp. 337–344, 2013.

T. Khairun Nisa’, Wuryanti, “Isolasi, Karakterisasi dan Amobilisasi α -Amilase dari Aspergillus niger FNCC 6018,” Integr. Clim. Prot. Cult. Herit. Asp. Policy Dev. Plans. Free Hanseatic City Hambg., vol. 26, no. 4, pp. 1–37, 2013.

E. Nurhartadi and E. S. Rahayu, “Isolasi dan karakterisasi yeast amilolitik dari ragi tape isolation and characterization of amylolytic yeast from ragi tape,” J. Teknol. Has. Pertan., vol. IV, no. 1, pp. 66–73, 2011.

N. Ohno et al., “Purification and Properties of Amylases Extracellularly Produced by an Imperfect Fungus, Fusidium sp. BX-1 in a Glycerol Medium,” Biosci. Biotechnol. Biochem., vol. 56, no. 3, pp. 465–471, 1992, doi: 10.1271/bbb.56.465.

R. Zonouzi, K. Khajeh, M. Monajjemi, and N. Ghaemi, “Role of the salt bridge between Arg176 and Glu126 in the thermal stability of the Bacillus amyloliquefaciens α-amylase (BAA),” J. Microbiol. Biotechnol., vol. 23, no. 1, pp. 7–14, 2013, doi: 10.4014/jmb.1205.05062.

M. Technik, T. M. Basis, B. Diseases, R. Manuscript, and R. December, “Calcium Binding in a-Amylases: An X-ray Diffraction Study at 2.1,” pp. 6244–6249, 1990.

S. Babacan and A. G. Rand, “Characterization of honey amylase,” J. Food Sci., vol. 72, no. 1, pp. C050–C055, 2007, doi: 10.1111/j.1750-3841.2006.00215.x.

A. Safari et al., “Penggunaan Enzim α-Amilase dari Saccharomycopsis fibuligera R64 untuk Peningkatan Kualitas Roti Komposit Terigu-Ubi Jalar Ungu,” Al-Kimia, vol. 5, no. 2, pp. 193–207, 2017, doi: 10.24252/al-kimia.v5i2.3861.

D. R. Nagarajan, G. Rajagopalan, and C. Krishnan, “Purification and characterization of a maltooligosaccharide-forming α-amylase from a new Bacillus subtilis KCC103,” Appl. Microbiol. Biotechnol., vol. 73, no. 3, pp. 591–597, 2006, doi: 10.1007/s00253-006-0513-4.

Z.-Q. Yang, Y.-N. Li, Z.-F. Zhang, Y. Wang, and G.-F. Shen, “[Expression of the gene coding for a thermostable alpha-amylase from Pyrococcus furious in Chiamydomonas reinhardtii chloroplast ],” Sheng Wu Gong Cheng Xue Bao, vol. 22, no. 4, p. 545—549, Jul. 2006, [Online]. Available: http://europepmc.org/abstract/MED/16894885.

T. Erban, M. Erbanova, M. Nesvorna, and J. Hubert, “The importance of starch and sucrose digestion in nutritive biology of synanthropic acaridid mites: α-amylases and α-glucosidases are suitable targets for inhibitor-based strategies of mite control,” Arch. Insect Biochem. Physiol., vol. 71, no. 3, pp. 139–158, 2009, doi: 10.1002/arch.20312.

S. Unji, Anharullah, and Muzuni, “Pengaruh Penambagan Enzim α-amilase Terhadap Karakteristik Sirup Glukosa dari Pati dan Ampas Sagu (Metroxilon Sp) dari Pengolahan Sagu Moramo Utara,” J. Sains dan Teknol. Pangan, vol. 1, no. 3, pp. 255–263, 2016.

M. Ueda, T. Asano, M. Nakazawa, K. Miyatake, and K. Inouye, “Purification and characterization of novel raw-starch-digesting and cold-adapted α-amylases from Eisenia foetida,” Comp. Biochem. Physiol. - B Biochem. Mol. Biol., vol. 150, no. 1, pp. 125–130, 2008, doi: 10.1016/j.cbpb.2008.02.003.

D. G. Syed, D. Agasar, and A. Pandey, “Production and partial purification of α-amylase from a novel isolate Streptomyces gulbargensis,” J. Ind. Microbiol. Biotechnol., vol. 36, no. 2, pp. 189–194, 2009, doi: 10.1007/s10295-008-0484-9.

B. L. Tee and G. Kaletunç, “Immobilization of a thermostable α-amylase by covalent binding to an alginate matrix increases high temperature usability,” Biotechnol. Prog., vol. 25, no. 2, pp. 436–445, 2009, doi: 10.1002/btpr.117.

J. Y. Damián-Almazo, A. Moreno, A. López-Munguía, X. Soberón, F. González-Muñoz, and G. Saab-Rincón, “Enhancement of the alcoholytic activity of α-amylase AmyA from Thermotoga maritima MSB8 (DSM 3109) by site-directed mutagenesis,” Appl. Environ. Microbiol., vol. 74, no. 16, pp. 5168–5177, 2008, doi: 10.1128/AEM.00121-08.

Y. chuan Wang, N. Zhao, J. wen Ma, J. Liu, Q. juan Yan, and Z. qiang Jiang, “High-level expression of a novel α-amylase from Thermomyces dupontii in Pichia pastoris and its application in maltose syrup production,” Int. J. Biol. Macromol., vol. 127, pp. 683–692, 2019, doi: 10.1016/j.ijbiomac.2019.01.162.

A. M. Fuadi, “<1.1.1.1.688.Pdf>,” vol. 12, no. 2, pp. 123–128, 2008.

S. Silaban and P. Simamora, “Isolasi dan Karakterisasi Bakteri Penghasil Amilase dari Sampel Air Tawar Danau Toba,” EduChemia (Jurnal Kim. dan Pendidikan), vol. 3, no. 2, p. 222, 2018, doi: 10.30870/educhemia.v3i2.3438.

I. Funke and M. F. Melzig, “Effect of different phenolic compounds on α-amylase activity: Screening by microplate-reader based kinetic assay,” Pharmazie, vol. 60, no. 10, pp. 796–797, 2005.

R. Tundis, M. R. Loizzo, and F. Menichini, “Natural Products as α-Amylase and α-Glucosidase Inhibitors and their Hypoglycaemic Potential in the Treatment of Diabetes: An Update,” Mini-Reviews Med. Chem., vol. 10, no. 4, pp. 315–331, 2010, doi: 10.2174/138955710791331007.

B. Wahyuntari, “Penghambat α-amilase: Jenis, Sumber, Dan Potensi Pemanfaatannya Dalam Kesehatan,” Lab. Pengemb. Teknol. Ind. Agro-Biomedika, vol. XXII, no. 2, pp. 197–201, 2011, [Online]. Available: http://download.portalgaruda.org/article.php?article=5639&val=205.

N. K. Soni et al., “A Review of Digestive Enzyme and Probiotic Supplementation for Functional Gastrointestinal Disorders,” vol. 73, no. 3, pp. 35–39, 2020.

O. C. Swami and N. J. Shah, “Functional dyspepsia and the role of digestive enzymes supplement in its therapy,” Int. J. Basic Clin. Pharmacol., vol. 6, no. 5, p. 1035, 2017, doi: 10.18203/2319-2003.ijbcp20171653.

U. R. Ernawati, L. U. Khasanah, and R. B. K. Anandito, “The Effect of Variation Dextrose Equivalents Maltodextrin Values on the Microencapsulant Characteristic of Teak Leaves (Tectona Grandis L.f) Natural Dye,” J. Teknol. Pertan., vol. 15, no. 2, pp. 111–120, 2014.

Meriatna, “HIDROLISA TEPUNG SAGU MENJADI MALTODEKTRIN MENGGUNAKAN ASAM KLORIDA Meriatna,” J. Teknol. Kim. Unimal, vol. 2, no. Mei, pp. 38–48, 2013.

Y. Dumoulin, L. H. Cartilier, and M. A. Mateescu, “Cross-linked amylose tablets containing α-amylase: An enzymatically-controlled drug release system,” J. Control. Release, vol. 60, no. 2–3, pp. 161–167, 1999, doi: 10.1016/S0168-3659(99)00065-6.

R. A. Arfah, A. Ahmad, S. Dali, M. N. Djide, Mahdalia, and A. R. Arif, “Utilization of α-amylase enzyme from Bacillus stearothermophilus RSAII1B for maltodextrin production from sago starch,” J. Phys. Conf. Ser., vol. 979, no. 1, 2018, doi: 10.1088/1742-6596/979/1/012018.

M. Pentury, H. Nursyam, N. Harahap, and S. Soemarno, “Karakterisasi Maltodekstrin Dari Pati Hipokotil Mangrove (Bruguiera Gymnorrhiza) Menggunakan Beberapa Metode Hidrolisis Enzim,” Indones. Green Technol. J., vol. 2, no. 1, pp. 53–60, 2013.

A. Laga, A. Dirpan, and A. A. Anshari, “PENGARUH KONSENTRASI SUBSTRAT PADA PEMBUATAN MALTODEKSTRIN DARI SUBSTRAT PATI SAGU (Effect Of Substrate Concentration Variation In Maltodextrin Production From Sago Starch),” pp. 23–30.




DOI: https://doi.org/10.52447/inrpj.v6i1.4517

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