Comparison of the Wild-Type α-Amylase and Its Variant Enzymes in Bacillus amyloliquefaciens in Activity and Thermal Stability, and Insights into Engineering the Thermal Stability of Bacillus α-Amylase

Lee, Seunjae; Mouri, Yoshiki; Minoda, Masashi; Oneda, Hiroshi; Inouye, Kuniyo

doi:10.1093/jb/mvj107

Cited by 36 publications

(19 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The higher liquefaction of cellulose due to enzyme activity at pH 6.5 to 7.5 was reported by many workers ( Malek et al1987, Araujo and Ward 1990, Hachiro and Kazuhiko 1991, Shailendra et al 1991, Hossain et al 1998, Hossain et al1999.The higher liquefaction of cellulose due to enzyme activity at 50˚C was reported by Kaneko et al 2005 andLee et al 2006. This observation also showed similarities with their reports.…”

Section: Effects Of Medium Ph and Temperaturesupporting

confidence: 85%

Isolation, identification and characterization of four cellulolytic actinomycetes and their cellulases

Alam

Sultana

Anwar

2013

Chittagong Univ. J. B. Sci.

View full text Add to dashboard Cite

Four highly cellulolytic actinomycetous isolates namely SG 1 , SG 2 , SG 3 and SS 1 were isolated from soil samples and provisionally identified as Streptomyces almquistii, S. caeruleus , S. hirsutus and S. endus, respectively. All the isolates showed heavy growth and liquefaction at 50˚C and pH 6.5 in Winstead's medium having 1.2% of CMC. The isolates were allowed to grow in Winstead's medium having Asparagine as a nitrogen source with different carbon sources for the maximum production of cellulases. The extracellular protein of the culture supernatant ranged from 1.14 μg /ml (SG 1 ) to 879.39 μg /ml (SG 3 ). The reducing sugar level of the culture supernatant ranged from 0.76 μg /ml (SG 2 ) to 558.33 μg /ml (SG 1 ). The highest CMC-ase activity (1431.81U/ml) was found with the crude enzyme of the strain SG 3 . The highest FP-ase activity (1087.11 U/ml) and Avicelase activity (1287.87U/ml) were found with the crude enzyme of SS 1 . To detrermine the optimum nitrogen sources, the isolates were allowed to grow in Winstead's medium having saw dust for SG 1 and SG 3 , dry leaf for SS 1 and SG 2 as a carbon source with different nitrogen sources for the maximum production of cellulases. The extracellular protein of the culture supernatant ranged from 35.50 μg /ml (SG 1 ) to 328.62 μg /ml (SS 1 ) and the reducing sugar level of the culture supernatant ranged from 3.79 μg /ml (SG 1 ) to 114.39 μg /ml (SG 3 ). However the highest CMC-ase activity (1353.78 U/ml), and FP-ase activity (215.90 U/ml) were found with the crude enzyme of the strain SG 2 and Avicelase activity (356.06U/ml) was found with the crude enzyme of the isolate SS 1 .

show abstract

Section: Effects Of Medium Ph and Temperaturesupporting

confidence: 85%

Isolation, identification and characterization of four cellulolytic actinomycetes and their cellulases

Alam

Sultana

Anwar

2013

Chittagong Univ. J. B. Sci.

View full text Add to dashboard Cite

show abstract

“…Recently, a new type of Bacillus α-amylase (Amy K38), a calcium-free amylase, was reported, and two sodium ions, instead of calcium ions, are used to retain the structure and function of this enzyme [59]. This report suggests that the interaction modes of BAA enzymes with ions are diverse.…”

Section: [15]mentioning

confidence: 99%

α-Amylase: An Ideal Representative of Thermostable Enzymes

Prakash

Jaiswal

2009

Appl Biochem Biotechnol

167

View full text Add to dashboard Cite

The conditions prevailing in the industrial applications in which enzymes are used are rather extreme, especially with respect to temperature and pH. Therefore, there is a continuing demand to improve the stability of enzymes and to meet the requirements set by specific applications. In this respect, thermostable enzymes have been proposed to be industrially relevant. In this review, alpha-amylase, a well-established representative of thermostable enzymes, providing an attractive model for the investigation of the structural basis of thermostability of proteins, has been discussed.

show abstract

“…Enzymes from hyperthermophilic bacteria include α-amylases from Desulfurococcus mucosus, Pyrodictium abyssi, Pyrococcus woesei, Pyrococcus furiosus, Thermococcus profundus, Thermococcus hydrothermalys [19] that all have optimal activity at 100°C. One of the most characterized α -amylases originates from Bacillus licheniformis, with optimal activity between 85 and 90°C [56], and in addition several engineered variants are developed and commercialized by Dupont (previously Genencor) such as Multifect AA 21L ® , and Novozymes (such as Termamyl ® and Liquozyme ® ) [16].…”

Section: Major Bottlenecksmentioning

confidence: 99%

Thermostable Glycoside Hydrolases in Biorefinery Technologies

Linares-Pastén¹,

Andersson²,

Karlsson

2014

CBIOT

View full text Add to dashboard Cite

Glycoside hydrolases, which are responsible for the degradation of the major fraction of biomass, the polymeric carbohydrates in starch and lignocellulose, are predicted to gain increasing roles as catalysts in biorefining applications in the future bioeconomy. In this context, thermostable variants will be important, as the recalcitrance of these biomass-components to degradation often motivates thermal treatments. The traditional focus on degradation is also predicted to be changed into more versatile roles of the enzymes, also involving specific conversions to defined products. In addition, integration of genes encoding interesting target activities opens the possibilities for whole cell applications, in organisms allowing processing at elevated temperatures for production of defined metabolic products.In this review, we overview the application of glycoside hydrolases related to the biorefining context (for production of food, chemicals, and fuels). Use of thermostable enzymes in processing of biomass is highlighted, moving from the activities required to act on different types of polymers, to specific examples in today's processing. Examples given involve (i) monosaccharide production for food applications as well as use as carbon source for microbial conversions (to metabolites such as fuels and chemical intermediates), (ii) oligosaccharide production for prebiotics applications (iii) treatment for plant metabolite product release, and (iv) production of surfactants of the alkyl glycoside class. Finally future possibilities in whole cell biorefining are shown.

show abstract

Comparison of the Wild-Type α-Amylase and Its Variant Enzymes in Bacillus amyloliquefaciens in Activity and Thermal Stability, and Insights into Engineering the Thermal Stability of Bacillus α-Amylase

Cited by 36 publications

References 26 publications

Isolation, identification and characterization of four cellulolytic actinomycetes and their cellulases

Isolation, identification and characterization of four cellulolytic actinomycetes and their cellulases

α-Amylase: An Ideal Representative of Thermostable Enzymes

Thermostable Glycoside Hydrolases in Biorefinery Technologies

Contact Info

Product

Resources

About