Melola Discovery

← Melola Discovery

Jurnal

Isolasi Dan Karakterisasi α-amilase Isolat Bakteri Amilolitik Asidofilik Dari Taman Nasional Rawa Aopa Watumaohai

Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta) · Vol. ume No. 1 (2008) · hlm. 15–23

DOI
10.70561/ica.v1i1.2451
ISSN
2655-6049, 2085-014X
Terbit
2008-12-01
Penerbit
Hasanuddin University
Bahasa
en

Abstrak

Isolation and characterization α-amylase acidophilic amylolytic bacteria isolate from Rawa Aopa Watumohai National Park has been carried out. The aims of these studies are to know the characteristics of acidophilic amylolytic bacteria isolate, the optimum concentration of substrate and temperature α-amylase activity yielded, and specific activity in each enzyme purification steps. Activity of α-amylase was measured with DNS (Dinitrosalisilic acidI) method at λ 550 nm and the rate of protein enzyme was measured with Biuret method at λ 540 nm. The content of this research were obtained the isolate bacteria TR 1 which higher amylolytic activity is the colonies are pale-yellow with convexelevated, undulate, bacill sel, and negative Gram. The maximum activity and protein content obtained with (NH4)2SO4 extracted at 60% (w/v). The specific activity of α-amylase in crude extract was 0.038 U/mg enzyme, after extracted with (NH4)2SO4 60% (w/v) was 0.146 U/mg enzyme with purification fold 3.8, and after dialysis was 0.255 U/mg enzyme with purification fold 3.8, respectively. The optimum concentration of substrate (amylose) was 1.25% (w/v) and the optimum incubation temperature was 45oC.Keywords: Rawa Aopa Watumohai National Park, acidophilic amylolytic bacteria, α-amilase

Jaringan kolaborasi para penulis

40 penulis · 90 tautan kepenulisan bersama · menampilkan 40 yang paling banyak terhubung

Arahkan kursor atau ketuk sebuah nama untuk menyorot rekan penulisnya. Klik dua kali untuk membuka halaman penulis.

  • Universitas Halu Oleo
  • Hasanuddin University
  • Islamic University of Riau
  • Universitas Muhammadiyah Parepare
  • Afiliasi tidak diketahui
  • Organisasi berbeda
  • Organisasi sama
  • Afiliasi tidak diketahui
  • Garis lebih tebal = lebih banyak artikel bersama · lingkaran lebih besar = lebih banyak artikel
Tampilkan sebagai tabel
Rekan penulisOrganisasiArtikel bersama
Andi Noor KholidhaAfiliasi tidak diketahui2
Aulia FadhilahAfiliasi tidak diketahui2
Tien TienAfiliasi tidak diketahui2
Sjarif SubijaktoAfiliasi tidak diketahui2
Nur SulviyanaAfiliasi tidak diketahui1
Yusuf HamraAfiliasi tidak diketahui1
Agus CahyadiAfiliasi tidak diketahui1
Wa Ode Sitti IlmawatiAfiliasi tidak diketahui1
Hijria HijriaUniversitas Halu Oleo1
Fitria DewiAfiliasi tidak diketahui1
Wa Ode Nanang Trisna DewiAfiliasi tidak diketahui1
Emand Syapriawan TolanamyUniversitas Halu Oleo1
Agusrinal AgusrinalAfiliasi tidak diketahui1
Amiruddin EsoUniversitas Halu Oleo1
Agus SaifuddinAfiliasi tidak diketahui1
Sulastrianah SulastrianahAfiliasi tidak diketahui1
Rio KristianAfiliasi tidak diketahui1
Hafied CangaraHasanuddin University1
Andi Alimuddin UndeAfiliasi tidak diketahui1
Heri FirmansyahAfiliasi tidak diketahui1
Ahmad Fathan AniqAfiliasi tidak diketahui1
Suparto SupartoIslamic University of Riau1
Jose Gama SantosAfiliasi tidak diketahui1
Ellydar ChaidirAfiliasi tidak diketahui1
Abdullah AbdullahUniversitas Muhammadiyah Parepare1
Sri Wilda AlbetaAfiliasi tidak diketahui1
Riana AnggrainiAfiliasi tidak diketahui1
Yunia Frida AdelkaAfiliasi tidak diketahui1
Didi TarmadiAfiliasi tidak diketahui1
Muhammad Rasyidur RidhoAfiliasi tidak diketahui1
Saviska Luqyana FadiaAfiliasi tidak diketahui1
Sumiati SimanullangAfiliasi tidak diketahui1
Lina LestariUniversitas Halu Oleo1
Ida UsmanAfiliasi tidak diketahui1
La Ode RusmanAfiliasi tidak diketahui1
Desi ChrismiwahdaniAfiliasi tidak diketahui1
Ary Dean AmryAfiliasi tidak diketahui1

Afiliasi berasal dari OpenAlex; metadata OAI-PMH jurnal tidak memuatnya. Penulis tanpa ID OpenAlex dicocokkan berdasarkan nama, sehingga dua orang bisa tergabung atau satu orang bisa terpisah.

Sumber metadata: OAI-PMH (metadata jurnal) https://journal.unhas.ac.id/index.php/ica/oai, pertama di-harvest 5 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
<oai_dc:dc xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/  http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
	<dc:title xml:lang="en">Isolasi Dan Karakterisasi α-amilase Isolat Bakteri Amilolitik Asidofilik Dari Taman Nasional Rawa Aopa Watumaohai</dc:title>
	<dc:creator xml:lang="en">Raharjo, Sapto</dc:creator>
	<dc:creator xml:lang="en">Ardiansyah, Ardiansyah</dc:creator>
	<dc:creator xml:lang="en">Chahyadi, Agus</dc:creator>
	<dc:description xml:lang="en">Isolation and characterization α-amylase acidophilic amylolytic bacteria isolate from Rawa Aopa Watumohai National Park has been carried out. The aims of these studies are to know the characteristics of acidophilic amylolytic bacteria isolate, the optimum concentration of substrate and temperature α-amylase activity yielded, and specific activity in each enzyme purification steps. Activity of α-amylase was measured with DNS (Dinitrosalisilic acidI) method at λ 550 nm and the rate of protein enzyme was measured with Biuret method at λ 540 nm. The content of this research were obtained the isolate bacteria TR 1 which higher amylolytic activity is the colonies are pale-yellow with convexelevated, undulate, bacill sel, and negative Gram. The maximum activity and protein content obtained with (NH4)2SO4 extracted at 60% (w/v). The specific activity of α-amylase in crude extract was 0.038 U/mg enzyme, after extracted with (NH4)2SO4 60% (w/v) was 0.146 U/mg enzyme with purification fold 3.8, and after dialysis was 0.255 U/mg enzyme with purification fold 3.8, respectively. The optimum concentration of substrate (amylose) was 1.25% (w/v) and the optimum incubation temperature was 45oC.Keywords : Rawa Aopa Watumohai National Park, acidophilic amylolytic bacteria, α-amilase</dc:description>
	<dc:publisher xml:lang="en">Hasanuddin University</dc:publisher>
	<dc:date>2008-12-01</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en">Peer-reviewed Article</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.unhas.ac.id/index.php/ica/article/view/2451</dc:identifier>
	<dc:identifier>10.70561/ica.v1i1.2451</dc:identifier>
	<dc:source xml:lang="en">Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta); Volume 1 No 1 - December 2008; 15-23</dc:source>
	<dc:source>2655-6049</dc:source>
	<dc:source>2085-014X</dc:source>
	<dc:language>en</dc:language>
	<dc:relation>https://journal.unhas.ac.id/index.php/ica/article/view/2451/1328</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2017 Indonesia Chimica Acta</dc:rights>
</oai_dc:dc>