Abstract:
:Two novel glycosyl hydrolase family 5 (GH5) β-mannanases (AoMan5A and AoMan5B) were identified from Aspergillus oryzae RIB40 by genome mining. The AoMan5A contains a predicted family 1 carbohydrate binding module (CBM-1), located at its N-terminal. The AoMan5A, AoMan5B and truncated mutant AoMan5AΔCL (truncating the N-terminal CBM and linker of AoMan5A) were expressed retaining the N-terminus of the native protein in Pichia pastoris GS115 by pPIC9KM. The specific enzyme activity of the purified reAoMan5A, reAoMan5B and reAoMan5AΔCL towards locust bean gum at pH 3.6 and 40°C for 10min, was 8.3, 104.2 and 15.8U/mg, respectively. The temperature properties of the reAoMan5AΔCL were improved by truncating CBM. They can degrade the pretreated konjac flour and produce prebiotics. In addition, they had excellent stability under simulative gastric fluid and simulative prilling process. All these properties make these recombinant β-mannanases potential additives for use in the food and feed industries.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Tang CD,Shi HL,Tang QH,Zhou JS,Yao LG,Jiao ZJ,Kan YCdoi
10.1016/j.enzmictec.2016.08.003subject
Has Abstractpub_date
2016-11-01 00:00:00pages
99-104eissn
0141-0229issn
1879-0909pii
S0141-0229(16)30147-8journal_volume
93-94pub_type
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