Production and Characterization of Cross-Linked Aggregates of Geobacillus thermoleovorans CCR11 Thermoalkaliphilic Recombinant Lipase

被引:7
作者
Oliart-Ros, Rosa-Maria [1 ]
Badillo-Zeferino, Giselle-Lilian [1 ]
Quintana-Castro, Rodolfo [2 ]
Ruiz-Lopez, Irving-Israel [3 ]
Alexander-Aguilera, Alfonso [2 ]
Dominguez-Chavez, Jorge-Guillermo [2 ]
Khan, Azmat Ali [4 ]
Nguyen, Dinh Duc [5 ,6 ]
Nadda, Ashok Kumar [7 ]
Sanchez-Otero, Maria-Guadalupe [2 ]
机构
[1] Tecnol Nacl Mexico, Inst Tecnol Veracruz, Unidad Invest & Desarrollo Alimentos, MA Quevedo 2779, Veracruz 91897, Ver, Mexico
[2] Univ Veracruzana, Fac Bioanal, Veracruz 91700, Ver, Mexico
[3] Benemerita Univ Autonoma Puebla, Fac Ingn Quim, Av San Claudio & 18 Sur,Ciudad Univ, Puebla 72570, Mexico
[4] King Saud Univ, Coll Pharm, Dept Pharmaceut Chem, Pharmaceut Biotechnol Lab, Riyadh 11451, Saudi Arabia
[5] Kyonggi Univ, Dept Environm & Energy Engn, 154-42 Gwanggyosan Ro, Suwon 16227, Gyeonggi Do, South Korea
[6] Nguyen Tat Thanh Univ, Fac Environm & Food Engn, 300A Nguyen Tat Thanh,Dist 4, Ho Chi Minh City 755414, Vietnam
[7] Jaypee Univ Informat Technol, Fac Biotechnol, Dept Biotechnol & Bioinformat, Solan 173234, Himachal Prades, India
来源
MOLECULES | 2021年 / 26卷 / 24期
关键词
cross-linked enzymatic aggregates (CLEAs); thermoalkaliphilic lipase; Geobacillus thermoleovorans; OPTIMIZED PREPARATION; THERMOSTABLE LIPASE; IMMOBILIZATION; BIOCATALYSTS; SUPPORT; GLUTARALDEHYDE; ESTERIFICATION; ESTERASE; BEHAVIOR; CLONING;
D O I
10.3390/molecules26247569
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Immobilization of enzymes has many advantages for their application in biotechnological processes. In particular, the cross-linked enzyme aggregates (CLEAs) allow the production of solid biocatalysts with a high enzymatic loading and the advantage of obtaining derivatives with high stability at low cost. The purpose of this study was to produce cross-linked enzymatic aggregates (CLEAs) of LipMatCCR11, a 43 kDa recombinant solvent-tolerant thermoalkaliphilic lipase from Geobacillus thermoleovorans CCR11. LipMatCCR11-CLEAs were prepared using (NH4)(2)SO4 (40% w/v) as precipitant agent and glutaraldehyde (40 mM) as cross-linker, at pH 9, 20 degrees C. A U-10(5(6)) uniform design was used to optimize CLEA production, varying protein concentration, ammonium sulfate %, pH, glutaraldehyde concentration, temperature, and incubation time. The synthesized CLEAs were also analyzed using scanning electron microscopy (SEM) that showed individual particles of <1 mu m grouped to form a superstructure. The cross-linked aggregates showed a maximum mass activity of 7750 U/g at 40 degrees C and pH 8 and retained more than 20% activity at 100 degrees C. Greater thermostability, resistance to alkaline conditions and the presence of organic solvents, and better durability during storage were observed for LipMatCCR11-CLEAs in comparison with the soluble enzyme. LipMatCCR11-CLEAs presented good reusability by conserving 40% of their initial activity after 9 cycles of reuse.
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页数:15
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