Purification and enzymatic identification of an acid stable and thermostable <i>α</i>-amylase from<i>Rhizopus microsporus</i>

Shen, Haiping; Mo, Xinying; Chen, Xia; Han, Dongyang; Chang-xin, Zhao

doi:10.1002/jib.45

Cited by 6 publications

(5 citation statements)

References 16 publications

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“…Considering the temperature-dependent binds between the enzymes and their polymeric substrates (starch and xylan), activation energies for hydrolyzing these substrates can be regarded as the apparent activation energy. Apparent activation energies (E a, app ) for starch and xylan hydrolysis by N. intermedia enzymes, in different ranges of temperature, are reported in Table 1 , which are comparable to the starch and xylan hydrolysis activation energy of Rhizopus microsporus amylase (34.3 kJ mol −1 ) [ 29 ] and Fusarium sp. xylanase (37.15 kJ mol −1 ) [ 30 ], respectively.…”

Section: Resultsmentioning

confidence: 70%

Amylase and Xylanase from Edible Fungus Neurospora intermedia: Production and Characterization

et al. 2019

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Integrated enzyme production in the biorefinery can significantly reduce the cost of the entire process. The purpose of the present study is to evaluate the production of two hydrolyzing enzymes (amylase and xylanase) by an edible fungus used in the biorefinery, Neurospora intermedia. The enzyme production was explored through submerged fermentation of synthetic media and a wheat-based waste stream (thin stillage and wheat bran). The influence of a nitrogen source on N. intermedia was investigated and a combination of NaNO3 and yeast extract has been identified as the best nitrogen source for extracellular enzyme production. N. intermedia enzymes showed maximum activity at 65 °C and pH around 5. Under these conditions, the maximum velocity of amylase and xylanase for starch and xylan hydrolysis was found to be 3.25 U mL−1 and 14.77 U mL−1, respectively. Cultivation of N. intermedia in thin stillage and wheat bran medium resulted in relatively high amylase (8.86 ± 0.41 U mL−1, 4.68 ± 0.23) and xylanase (5.48 ± 0.21, 2.58 ± 0.07 U mL−1) production, respectively, which makes this fungus promising for enzyme production through a wheat-based biorefinery.

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Section: Resultsmentioning

confidence: 70%

Amylase and Xylanase from Edible Fungus Neurospora intermedia: Production and Characterization

et al. 2019

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“…Similarly, GpA1 had a maximal activity at pH 6.0, whereas it retained almost 100% of its initial activity between pH 5.0 and 9.0, demonstrating that GpA1 has good acid and alkali resistance . Surprisingly, GpA1 was originated from psychrophile, but its optimum temperature reached up to 70°C, which was higher than that of common fungal amylases from mesophile microorganisms and even as high as that of many thermostable fungal amylases, such as R. microspores amylase . Nevertheless, the thermostability of GpA1 was comparatively lower than the common thermostable α‐amylase.…”

Section: Discussionmentioning

confidence: 94%

“…The enzyme showed over 70% of maximum activity at 50 and 60°C. The optimum temperature of GpA1 is similar to that of the thermostable amylase from thermophilic fungi Rhizopus microspores , which also exhibits optimal activity at 70°C . The effect of pH on the α‐amylase activity was studied at various pH values.…”

Section: Resultsmentioning

confidence: 99%

“…Nevertheless, the thermostability of GpA1 was comparatively lower than the common thermostable α‐amylase. For instance, Shen et al reported an thermostable α‐amylase from R. microspores with an optimal temperature of 70°C, but its half‐life at 60°C was 60 min, which was fourfold longer than that of GpA1 . However, the thermolability of GpA1 was as well as that of cold‐adapted enzyme ( e.g .…”

Section: Discussionmentioning

confidence: 99%

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A novel saccharifying α‐amylase of Antarctic psychrotolerant fungi Geomyces pannorum: Gene cloning, functional expression, and characterization

et al. 2015

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A DNA segment encoding a novel a-amylase was cloned from the Antarctic psychrotolerant fungi Geomyces pannorum. The gene has an open reading frame of 1761 bp, deduced 586 amino acids, revealing a relatively low homology to a-amylases from diverse fungal genera. The a-amylase gene was overexpressed in Pichia pastoris, and the recombinant a-amylase was purified and characterized. Enzymatic activity was optimal at pH 6.0 and 70°C, and the specific activity was 9.78 Â 10 3 U/mg when using soluble starch as substrate. Moreover, the enzyme retained more than 90% of its maximum activity over a wide pH range (6.0-9.0). Exceptionally, the main hydrolysis products of soluble starch catalyzed by the enzyme were glucose and maltose, of which glucose reached a concentration of 68.8% (w/w). This is the first report on identifying thermophilic fungal amylase from psychrotolerant fungi. Also, the preliminary study on the high-glucose-producing a-amylase with detailed enzymatic properties shows a potential application prospect in syrup industry.

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“…The gel strength of the gelatin extract was measured as described by Boran and Regenstein [32] with some modifications, employing a Perten Instruments TVT 6700 texturometer (PerkinElmer Company, Sydney, Australia) equipped with a 40 mm diameter flag compression. Gelatin (6.67%) was dissolved in distilled water at 45°C, introduced into 100 mL containers measuring 60 mm in height and 50 mm in diameter and then cooled to 7°C over a period of 15 hours.…”

Section: Gel Strengthmentioning

confidence: 99%

Valorization of Yellowfin Tuna Tails: An Approximation to Circular Bioeconomy

Sisa Allayca,

Martínez-Alvarez,

Gómez-Estaca

et al. 2024

Preprint

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This study investigates the valorization potential of yellowfin tuna tails for the production of high-value commercial products. Muscle and skins were firstly mechanically separated by using a specifically designed device. The muscle was then used as a nitrogen source for the growth of the proteolytic enzymes-producer Bacillus subtilis, whereas the skins were employed for gelatin extrac-tion. The proteases from Bacillus subtilis were partially purified and used to produce antioxidant peptides from gelatin obtained. The gelatin obtained formed a gel upon cooling, with gelling and melting temperatures at 16 ºC and 22 ºC, respectively, and Bloom Strength of ≈ 160. RSM was used to determine the optimal hydrolysis conditions to obtain the highest antioxidant activity (35.96%, measured as DPPH radical scavenging activity), which were 50°C / 6.5 IU of enzyme. The findings emphasize the importance of an integrated approach to maximize the value of tuna by-products, promoting sustainability in the frame of circular bioeconomy. Overall, these results contribute to the efficient utilization of tuna by-products, waste reduction, and enhance economic viability of the tuna industry.

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Purification and enzymatic identification of an acid stable and thermostable α-amylase fromRhizopus microsporus

Cited by 6 publications

References 16 publications

Amylase and Xylanase from Edible Fungus Neurospora intermedia: Production and Characterization

Amylase and Xylanase from Edible Fungus Neurospora intermedia: Production and Characterization

A novel saccharifying α‐amylase of Antarctic psychrotolerant fungi Geomyces pannorum: Gene cloning, functional expression, and characterization

Valorization of Yellowfin Tuna Tails: An Approximation to Circular Bioeconomy

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