Teknologi Indonesia
Vol 37, No 1 (2014)

PURIFICATION AND PROPERTIES OF MANNANASE FROM Aspergillus ustus BL5

Thontowi, Ahmad (Unknown)
Rahmani, Nanik (Unknown)
Andriani, Ade (Unknown)
Yopi, - (Unknown)



Article Info

Publish Date
24 Feb 2015

Abstract

Strain of BL5 was reported as a mannanase producer. The purposes of this study are identification, purification and characterization of mannanase from BL5. The Internal Transcribed Spacer (ITS) regions analysis showed that BL5 strain have 93% similarity with Aspergillus ustus isolate UOA/HCPF 9236. An extracellular mannanase from the culture supernatant of a fungus A. ustus BL5 was purified. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 50 to 51 kDa. The mannanase exhibited optimum catalytic activity at pH 7.0 and 55C. The metal ions Ca2+, Cu2+ and SDS inhibited complete enzyme activity. The metal ion Mg2+ and EDTA increased complete enzyme activity. The value of Vmax = 5,88 ?mol mannose/min/ml and Kmax = 0.64 mg/ml. Mannanase of A. ustus BL5 be able to hydrolyzed porang mannan.

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Journal Info

Abbrev

JTI

Publisher

Subject

Computer Science & IT

Description

JTI is a journal in the Departement of Engineering Sciences - Indonesian Institute of Sciences (LIPI). JTI has policy to publish a new and original research paper or a review paper in The scope of Technology. JTI publishes two issues per year. The journal has been registered with printed-ISSN ...