Characterization of the native form and the carboxy‐terminally truncated halotolerant form of α‐amylases from <i>Bacillus subtilis</i> strain FP‐133

Takenaka, Shinji; Miyatake, Ayaka; Tanaka, Kosei; Kuntiya, Ampin; Techapun, Charin; Leksawasdi, Noppol; Seesuriyachan, Phisit; Chaiyaso, Thanongsak; Watanabe, Masanori; Yoshida, Ken-ichi

doi:10.1002/jobm.201400813

Cited by 23 publications

(13 citation statements)

References 34 publications

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“…Halo-tolerance is an important property of industrial enzymes (Yan et al, 2009;Takenaka et al, 2015). Halophilicity may be attributed to the ability of the protein amino acid residues to resist the destabilizing effect of surrounding electrolytes, and most of the halo-tolerant proteins have been described to have similar sequences dominated by acidic residues (Graziano and Merlino, 2014).…”

Section: Modification For Halophilicity and Thermostabilitymentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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The search for novel renewable products over synthetics hallmarked this decade and those of the recent past. Most economies that are prospecting on biodiversity for improved bio-economy favor renewable resources over synthetics for the potential opportunity they hold. However, this field is still nascent as the bulk of the available resources are non-renewable based. Microbial metabolites, emphasis on secondary metabolites, are viable alternatives; nonetheless, vast microbial resources remain under-exploited; thus, the need for a continuum in the search for new products or bio-modifying existing products for novel functions through an efficient approach. Environmental distress syndrome has been identified as a factor that influences the emergence of genetic diversity in prokaryotes. Still, the process of how the change comes about is poorly understood. The emergence of new traits may present a high prospect for the industrially viable organism. Microbial enzymes have prominence in the bio-economic space, and proteases account for about sixty percent of all enzyme market. Microbial keratinases are versatile proteases which are continuously gaining momentum in biotechnology owing to their effective bio-conversion of recalcitrant keratin-rich wastes and sustainable implementation of cleaner production. Keratinase-assisted biodegradation of keratinous materials has revitalized the prospects for the utilization of cost-effective agro-industrial wastes, as readily available substrates, for the production of high-value products including amino acids and bioactive peptides. This review presented an overview of keratin structural complexity, the potential mechanism of keratin biodegradation, and the environmental impact of keratinous wastes. Equally, it discussed microbial keratinase; vis-à-vis sources, production, and functional properties with considerable emphasis on the ecological implication of microbial producers and catalytic tendency improvement strategies. Keratinase applications and prospective high-end use, including animal hide processing, detergent formulation, cosmetics, livestock feed, and organic fertilizer production, were also articulated.

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Section: Modification For Halophilicity and Thermostabilitymentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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“…This strongly suggests that Amy2 and Amy3 could be derived from the proteolytic degradation of Amy 1, which may be due to the secreted proteolytic activity in the extracellular medium of the US586 strain. Moreover, it was demonstrated that the production of amylases isoforms by proteolysis had already been described for B. subtilis X‐23 (Kohji et al, ) and B. subtilis FP‐133 (Takenaka et al, ) displaying the same physicochemical properties.…”

Section: Resultsmentioning

confidence: 90%

The optimized production, purification, characterization, and application in the bread making industry of three acid‐stable alpha‐amylases isoforms from a new isolated Bacillus subtilis strain US586

et al. 2019

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A new alpha‐amylase‐producing strain was assigned as Bacillus subtilis US586. The used statistical methodology indicated that amylase production was enhanced by 5.3 folds. The crude enzyme analysis proved the presence of three amylases isoforms Amy1, Amy2, and Amy3 called Amy586. The purified amylases had molecular masses of 48, 52, and 68 kDa with a total specific activity of 2,133 U/mg. Amy586 generated maltose, maltotriose, and maltopentaose as main final products after starch hydrolysis. It exhibited a large 4–6 optimal pH, a 60°C temperature activity, and a moderate thermostability. Amy586 displayed a high pH stability ranging from 3.5 to 6. The addition of Amy586 to weak wheat flour decreased its P/L ratio from 1.9 to 1.2 and increased its dough baking strength (W) from 138 × 10−4 to 172 × 10−4 J. Amy586 also improved the bread texture parameters by reducing its firmness and boosting the cohesion and elasticity values. Practical applications Bacterial alpha‐amylases with novel properties have been the major extent of recent research. In this paper, we managed to demonstrate that the addition of a purified amylolytic extract from the new isolated Bacillus subtilis strain US586 to weak local flour improves dough rheological proprieties and bread quality. Therefore, Amy586 can be considered as a bread making improver.

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“…Anti-salt or halotolerance is an important characteristic to evaluate whether the enzyme can be used in industrial processes1829. We used different concentrations of NaCl to monitor the halotolerance of KerSMD and its different variants (Fig.…”

Section: Resultsmentioning

confidence: 99%

Improved catalytic efficiency, thermophilicity, anti-salt and detergent tolerance of keratinase KerSMD by partially truncation of PPC domain

Fang

Zhang

et al. 2016

Sci Rep

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The keratinase from Stenotrophomonas maltophilia (KerSMD) is known for its high activity and pH stability in keratin degradation. However, catalytic efficiency and detergent tolerability need to be improved in order to be used for industrial application. In this work, we obtained several keratinase variants with enhanced catalytic efficiency, thermophilicity, and anti-salt and detergent tolerability by partially truncating the PPC domain of KerSMD. The variants all showed improved catalytic efficiency to synthetic substrate AAPF, with the V355 variant having the highest kcat /Km value of 143.6 s−1 mM−1. The truncation of keratinase had little effect on alkaline stability but obviously decreased collagenase activity, developing its potential application in leather treatment. The variants V380, V370, and V355 were thermophilic, with a 1.7-fold enhancement of keratinlytic activity at 60 °C when compared to the wild type. The entire truncation of PPC domain obtained the variant V355 with improved tolerance to alkalinity, salt, chaotropic agents, and detergents. The V355 variant showed more than a 40% improvement in activity under 15% (w/v) NaCl or 4% (w/v) SDS solution, showing excellent stability under harsh washing and unhairing conditions. Our work investigated how protein engineering affects the function of PPC domain of KerSMD.

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Characterization of the native form and the carboxy‐terminally truncated halotolerant form of α‐amylases from Bacillus subtilis strain FP‐133

Cited by 23 publications

References 34 publications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

The optimized production, purification, characterization, and application in the bread making industry of three acid‐stable alpha‐amylases isoforms from a new isolated Bacillus subtilis strain US586

Improved catalytic efficiency, thermophilicity, anti-salt and detergent tolerance of keratinase KerSMD by partially truncation of PPC domain

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