scholarly journals Characteristics and Role of Feruloyl Esterase from Aspergillus Awamori in Japanese Spirits, ‘Awamori’ Production

10.5772/31190 ◽  
2012 ◽  
Author(s):  
Makoto Kanauchi
Keyword(s):  
Feruloyl Esterase ◽  
Aspergillus Awamori

Role of bacterial virulence proteins in Agrobacterium-mediated transformation of Aspergillus awamori

2004 ◽  
Vol 41 (5) ◽  
pp. 571-578 ◽  
Author(s):  
C.B. Michielse ◽  
A.F.J. Ram ◽  
P.J.J. Hooykaas ◽  
C.A.M.J.J.van den Hondel
Keyword(s):  
Bacterial Virulence ◽  
Aspergillus Awamori ◽  
Agrobacterium Mediated Transformation ◽  
Virulence Proteins

scholarly journals A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan

2019 ◽  
Vol 294 (46) ◽  
pp. 17339-17353 ◽  
Author(s):  
Jesper Holck ◽  
Folmer Fredslund ◽  
Marie S. Møller ◽  
Jesper Brask ◽  
Kristian B. R. M. Krogh ◽  
...  
Keyword(s):  
Wastewater Treatment ◽  
Surface Plasmon Resonance ◽  
Feruloyl Esterase ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Surface Plasmon Resonance Analysis ◽  
Resonance Analysis ◽  
Feruloyl Esterases ◽  
Folded Proteins

Feruloyl esterases (EC 3.1.1.73), belonging to carbohydrate esterase family 1 (CE1), hydrolyze ester bonds between ferulic acid (FA) and arabinose moieties in arabinoxylans. Recently, some CE1 enzymes identified in metagenomics studies have been predicted to contain a family 48 carbohydrate-binding module (CBM48), a CBM family associated with starch binding. Two of these CE1s, wastewater treatment sludge (wts) Fae1A and wtsFae1B isolated from wastewater treatment surplus sludge, have a cognate CBM48 domain and are feruloyl esterases, and wtsFae1A binds arabinoxylan. Here, we show that wtsFae1B also binds to arabinoxylan and that neither binds starch. Surface plasmon resonance analysis revealed that wtsFae1B's Kd for xylohexaose is 14.8 μm and that it does not bind to starch mimics, β-cyclodextrin, or maltohexaose. Interestingly, in the absence of CBM48 domains, the CE1 regions from wtsFae1A and wtsFae1B did not bind arabinoxylan and were also unable to catalyze FA release from arabinoxylan. Pretreatment with a β-d-1,4-xylanase did enable CE1 domain-mediated FA release from arabinoxylan in the absence of CBM48, indicating that CBM48 is essential for the CE1 activity on the polysaccharide. Crystal structures of wtsFae1A (at 1.63 Å resolution) and wtsFae1B (1.98 Å) revealed that both are folded proteins comprising structurally-conserved hydrogen bonds that lock the CBM48 position relative to that of the CE1 domain. wtsFae1A docking indicated that both enzymes accommodate the arabinoxylan backbone in a cleft at the CE1–CBM48 domain interface. Binding at this cleft appears to enable CE1 activities on polymeric arabinoxylan, illustrating an unexpected and crucial role of CBM48 domains for accommodating arabinoxylan.

scholarly journals Role of phosphate solubilizing fungi during phosphocompost production and their effect on the growth of tomato (Lycopersicon esculentum L) plants

2011 ◽  
Vol 3 (2) ◽  
pp. 287-290 ◽  
Author(s):  
G . Sibi
Keyword(s):  
Plant Growth ◽  
Rock Phosphate ◽  
Trichoderma Viride ◽  
Nutrient Content ◽  
Aspergillus Awamori ◽  
Low Grade ◽  
Nutrient Value ◽  
P Content ◽  
Phosphate Solubilizing

Experiments were conducted to evaluate the effect of phosphate solubilizing fungi (Aspergillus awamori and Trichoderma viride) in phosphocompost preparation along with low grade rock phosphate. Co-inoculation of phosphate-solubilizing fungi significantly increased the nutrient value of the compost that explores high P-solubilizing potential of A.awamori and T.viride which can be exploited for the solubilization of fixed phosphates thereby enhancing soil fertility and plant growth. Rock phosphate application along with phosphate solubilizing fungi increased 69.2% acid phosphatase and 65% alkaline phosphatase activity over ordinary compost. With co-inoculation, maximum P content (64.3%) was observed followed by single inoculation with A.awamori (62.2%). The present findings revealed that phosphate solubilizing fungi can interact positively in promoting nutrient content of compost and plant growth leading to improved yield.

Sign in / Sign up

Export Citation Format

Share Document