PENINGKATAN KESTABILAN ENZIM α- AMILASE DARI Aspergillus niger L-51 DENGAN MODIFIKASI KIMIA MENGGUNAKAN SITRAKONAT ANHIDRIDA

Ni Putu Naris Berdianti, (1327011029) (2015) PENINGKATAN KESTABILAN ENZIM α- AMILASE DARI Aspergillus niger L-51 DENGAN MODIFIKASI KIMIA MENGGUNAKAN SITRAKONAT ANHIDRIDA. Other thesis, UNIVERSITAS LAMPUNG.

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Abstrak

Penelitian ini dilakukan dengan tujuan untuk meningkatkan kestabilan enzim α- amilase dari Aspergillus niger L-51 dengan modifikasi kimia. Penelitian ini dilakukan dengan beberapa tahapan yaitu isolasi, pemurnian dan modifikasi kimia. Isolasi enzim dilakukan dengan menggunakan sentrifugasi dingin, pemurnian enzim menggunakan fraksinasi amonium sulfat dan dialisis, sedangkan modifikasi kimia menggunakan sitrakonat anhidrida. Aktivitas enzim α-amilase ditentukan dengan metode Fuwa dan metode Mandels, sedangkan metode Lowry digunakan untuk menentukan kadar protein enzim. Derajat modifikasi ditentukan dengan menggunakan asam trinitrobenzena sulfonat (TNBS). Hasil penelitian menunjukan suhu optimum enzim hasil pemurnian adalah 50oC, pH optimum 5,5; KM = 5,614 mg/ml substrat, dan Vmaks = 175,438 μmol/ml.menit. Stabilitas termal enzim hasil pemurnian ditunjukan dengan nilai t1/2 = 60,261 menit, ki = 0,0115 menit-1, dan ΔGi 102,318 kJ mol-1. Suhu optimum enzim hasil modifikasi (32%, 49% dan 61% ) adalah 50oC, pH optimum 5,5; Stabilitas termal enzim hasil modifikasi (32%, 49% dan 61%) ditunjukan dengan nilai t 1/2 = 77,865 menit, 79,655 menit, dan 84,512 menit. Nilai ki = 0,0089 menit-1, 0,0087 menit-1, 0,0082 menit-1. Sedangkan nilai ΔGi = 102,968 kJ mol-1, 103,029 kJ mol-1 dan 103,032 kJ mol-1. Berdasarkan penurunan nilai ki, modifikasi kimia enzim α-amilase dari Aspergillus niger L-51 dengan menggunakan sitrakonat anhidrida dapat meningkatkan kestabilan enzim antara 1,2 – 1,4 kali dibandingkan enzim hasil pemurnian. Kata kunci : Aspergillus niger L-51, α-Amilase, modifikasi kimia, sitrakonat anhidrida ABSTRAK BAHASA INGGRIS This research was aimed to study the effect of chemical modification on the thermal stability of α-amylase from local fungi isolate Aspergillus niger L-51 which. To achieve this aim, isolation purification, and chemical modification of the enzyme were performed. Enzyme was purified by ammonium sulphate fractionation and dialysis, and followed by chemical modification with citraconic anhydride. The α-amilase activity was measured by Fuwa method and Mandels method, protein consentration was measured by Lowry method, while the modification degree was measured by using trinitrobenzen sulfonac acid (TNBS). The results showed that the optimum temperature of the native enzyme was 50˚C; optimum pH= 5.5; KM = 5.614 mg/ml substrate, and Vmaks = 175.438 μmol/ml.minute. The thermal stability of the native enzyme has data of: t1/2 = 60.261 min, ki = 0.0115 min-1, ΔGi 102.318 kJ mole-1. The modified enzymes with citraconic anhydride with modification degree of 32; 49; and 61% showed the optimum temperature and optimum pH, KM, Vmaks, t ½ , ki, ΔGi i.e: 50˚C, 5.5, 6.734 mg/mL substrate, 156.250 μmol/mL.minute, 77.865 minute, 0.0089 minute-1, 102.968 kJ mole-1; 50˚C, 5.5, 5.124 mg/mL substrate, 135.135 μmol/mL.minute, 79.655 minute, 0.0087 minute-1, 103.029 kJ mole-1; 50˚C, 5.5, 4,107 mg/mL substrate, 126.582 μmol/mL.minute, 84.512 minute, 0.0082 minute- 1, 103.032 kJ mole-1, respectively. While based on the decrease of ki values, the chemical modification on the native α-amylase has been able to increase the thermal stability up to 1.2 – 1.4 times compared to that of the native one. Keywords : Aspergillus niger L-51, α-amylase, chemical modification, citraconic anhydride

Tipe Karya Ilmiah: Tesis (Other)
Subyek: Q Science (General) > QD Chemistry
Program Studi: Fakultas MIPA > Prodi Magister Ilmu Kimia
Depositing User: 3038571 . Digilib
Date Deposited: 21 Jan 2016 03:10
Last Modified: 21 Jan 2016 03:10
URI: http://digilib.unila.ac.id/id/eprint/18790

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