Enhanced hydrolytic efficiency of an engineered CBM11-glucanase enzyme chimera against barley beta-D-glucan extracts

Author(s)

Furtado, Gilvan Pessoa ^[1] ; Carli, Sibeli ^[2] ; Meleiro, Luana Parras ^[2] ; Santos Salgado, Jose Carlos ^[2] ; Ward, Richard John ^[2]

Affiliation

^[1] Fundacao Oswaldo Cruz Fiocruz Ceara, Rua Sao Jose S-N, Eusebio, Ceara - Brazil

^[2] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, Ave Bandeirantes 3900, Ribeirao Preto, SP - Brazil

• Document type: Journal article
• Source: Food Chemistry; v. 365, DEC 15 2021.
• Web of Science Citations: 0

Abstract

The beta-D-glucans are abundant cell wall polysaccharides in many cereals and contain both (1,3)- and (1,4)-bonds. The beta-1,3-1,4-glucanases (EC 3.2.1.73) hydrolyze beta-(1,4)-D-glucosidic linkages in glucans, and have applications in both animal and human food industries. A chimera between the family 11 carbohydrate-binding module from Ruminoclostridium (Clostridium) thermocellum celH (RtCBM11), with the beta-1,3-1,4-glucanase from Bacillus subtilis (BglS) was constructed by end-to-end fusion (RtCBM11-BglS) to evaluate the effects on the catalytic function and its application in barley beta-glucan degradation for the brewing industry. The parental and chimeric BglS presented the same optimum pH (6.0) and temperature (50 degrees C) for maximum activity. The RtCBM11-BglS showed increased thermal stability and 30% higher hydrolytic efficiency against purified barley beta-glucan, and the rate of hydrolysis of beta-1,3-1,4-glucan in crude barley extracts was significantly increased. The enhanced catalytic performance of the RtCBM11-BglS may be useful for the treatment of crude barley extracts in the brewing industry. (AU)

• FAPESP's process: 16/17582-0 - Thermostability modulation of a ß-glucosidase stimulated by glucose and xylose using site directed glycosylation
• Grantee: Luana Parras Meleiro Garcia
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 16/24139-6 - Design and Characterization of Multifunctional Xylanolytic Enzymes
• Grantee: Richard John Ward
• Support Opportunities: Regular Research Grants
• FAPESP's process: 17/13734-3 - Engineering of an endopolygalacturonase by insertion of different Carbohydrate Binding Modules (CBMs): chimerogenesis and proximity effects
• Grantee: Sibeli de Carli
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 14/50884-5 - INCT 2014: National Institute of Science and Technology of Bioethanol
• Grantee: Marcos Silveira Buckeridge
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 19/21989-7 - Bioprospection of low molecular weight fungal enzymes involved in plant cell wall degradation
• Grantee: José Carlos dos Santos Salgado
• Support Opportunities: Scholarships in Brazil - Post-Doctoral