Production, partial purification and properties of β‐mannanases obtained by solid substrate fermentation of spent soluble coffee wastes and copra paste using
            <i>Aspergillus oryzae</i>
            and
            <i>Aspergillus niger</i>

Regalado, Carlos M.; García-Almendárez, Blanca E.; Venegas-Barrera, L. M.; Téllez‐Jurado, Alejandro; Rodríguez-Serrano, Gabriela; Huerta‐Ochoa, Sergio; Whitaker, John R.

doi:10.1002/1097-0010(200007)80:9<1343::aid-jsfa651>3.0.co;2-#

Cited by 37 publications

(25 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fungal mannanases, however, seem to vary more significantly in their mass. Aspergillus mannanases range from 30-110 kDa 24 while those of Trichoderma range from 32-46 kDa 25,26 . The optimum pH of mannanase S1 was similar to those of some bacterial and fungal mannanases which are in the range of 3.0-6.0 22,[26][27][28][29] .…”

Section: Discussionmentioning

confidence: 99%

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Chantorn¹,

Pongsapipatana²,

Keawsompong³

et al. 2013

ScienceAsia

View full text Add to dashboard Cite

The mannanase S1 from Klebsiella oxytoca KUB-CW2-3 was purified by a single anion exchange chromatography to electrophoretic homogeneity. S1 is a protein with a molecular mass of approximately 165 kDa and a pI value of 3.5. The optimum pH and temperature of mannanase activity were 4.0 and 40°C, respectively. The enzyme exhibited good stability over the broad pH range of 3-6. The mannanase S1 exhibited specific activity for different mannan substrates including galactomannan from locust bean gum (LBG), copra meal, and glucomannan from konjac, while neither xylanase nor cellulase activity were detectable. The Michaelis-Menten constants (Km), maximum velocity (Vmax), and the catalytic constant (kcat) values of S1 against LBG and konjac mannan were 1.038-1.056 mg/ml, 6.149-6.183 µU ml −1 min −1 , and 0.047 s −1 , respectively. In addition, mannanase activity was activated by Co 2+ (129%) but completely inhibited by EDTA and Zn 2+ . The N-terminal amino acid sequence (GRVGEAGPHGPHGPH) of mannanase S1is different from the N-terminal region of other bacterial mannanases belonging to the glycoside hydrolase family GH5. The degradation products of mannanase S1 from LBG hydrolysis were galactose and unknown oligosaccharides with a different molecular structure to mannobiose, triose, and tetraose indicating the cleavages of α-1,6-galactosidic and β-1,4-mannosidic linkages. Its hydrolysis of 100 mM CoCl2-treated copra mannan enhanced the growth of Lactobacillus reuteri KUB-AC5 but inhibited that of Salmonella serovar Enteritidis S003, indicating potential prebiotic properties by the action of mannanase from K. oxytoca.

show abstract

Section: Discussionmentioning

confidence: 99%

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Chantorn¹,

Pongsapipatana²,

Keawsompong³

et al. 2013

ScienceAsia

View full text Add to dashboard Cite

show abstract

“…Sieved CS was alkaline pre-treated using 4 g L -1 NaOH in a weight ratio 1:10 (CS:alkaline solution) for 12 hrs at room temperature and then excess NaOH was removed by rinsing with water until pH 7. Substrate moisture was adjusted to 800 g kg -1 by adding a solution of (Regalado et al 2000, Lagunas-Bernabé et al 2006.…”

Section: Cultures Conditionsmentioning

confidence: 95%

“…A. niger GS1 was kept as spore suspension in 0.1% Tween 20 on silica gel (3:1 weight ratio) at 4ºC. Stock cultures were sub-cultured on fresh sterile potato dextrose agar (PDA; Bioxon, Cuautitlán, Mexico) plates and incubated for 72-120 hrs at 30ºC (Regalado et al 2000).…”

Section: Materials and Microorganismmentioning

confidence: 99%

See 1 more Smart Citation

Xylanolytic enzymes production by Aspergillus niger GS1 from solid-state fermentation on corn stover and their effect on ruminal digestibility

Regalado‐González¹,

Vázquez-Obregón²,

García-Almendárez³

et al. 2011

Electro Journal of Biotech

Self Cite

View full text Add to dashboard Cite

Hemicellulosic agricultural by-products such as corn stover (CS) are highly available materials which represent an opportunity to develop value added products. Native Aspergillus niger GS1 was used for solid-state fermentation (SSF) on alkali pre-treated CS (ACS) aimed to optimize xylanolytic enzymes production, and their effect on in vitro ruminal and true digestibility of ACS. Enzyme production was empirically modelled using a fractional factorial design 2 9-5 , and the resulting significant factors were glucose, yeast extract and two mineral salts, which were arranged in a DraperLin optimization design at two levels. Predicted optimum xylanolytic activity of 33.6 U (mg protein) -1 was achieved at 48 hrs of SSF, and was validated by confirmatory experiments. ACS was incubated with a semipurified enzymatic extract (EE) showing a xylanolytic activity of 1600 U kg -1 dry ACS for 12 hrs before exposure to cow's ruminal liquid for 72 hrs, which led to 5% and 10% increase of in vitro ruminal and true digestibility, respectively. CS is a readily available by-product in different regions which after alkaline treatment and partial hydrolysis with the EE, may be advantageously used as supplement for ruminant feed.

show abstract

“…Bacterial -mannanases are mainly classiWed into GH 5-8 with alkaline pH optima, and -mannanases from eukaryota belong to GH 5-7 and 5-10 and act at acidic pHs [38]. Fungal -mannanases are mainly conWned into GH 5-7, and some of them can tolerate alkalinity up to pH 8.0 [6,22,32].…”

Section: Introductionmentioning

confidence: 99%

Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola insolens Y1

Luo

Wang

Huang

et al. 2012

Journal of Industrial Microbiology and Biotechnology

View full text Add to dashboard Cite

In this article, we firstly report a highly alkali-tolerant fungal β-mannanase from Humicola insolens Y1. The full-length cDNA of the β-mannanase, designated as man5A, has an open reading frame of 1,233 bp that encodes a 411-amino acid polypeptide (Man5A) with a calculated molecular mass of 42.3 kDa. The deduced sequence of Man5A comprises a putative 20-residue signal peptide and a catalytic domain belonging to glycoside hydrolase family 5, and displays 61-85% identities with hypothetical proteins and 32-39% with experimentally verified fungal β-mannanases. Purified recombinant Man5A produced by Pichia pastoris has a specific activity of 1,122 U mg⁻¹ and exhibits optimal activity at pH 5.5 and 70°C. Distinct from other reported fungal β-mannanases, Man5A is highly alkali tolerant, exhibiting 45 and 36% of the maximal activity at pH 8.0 and 9.0, respectively, and more than 10% activity even at pH 10.0. Moreover, Man5A has excellent pH stability at pH 5.0-12.0 and is highly thermostable at 50°C. The higher frequency of alkaline amino acids (Arg and Lys), greater pKa values of the catalytic residues, and more positively charged residues on the surface of Man5A might be the causes. Man5A has strong resistance to various neutral and alkaline proteases, retaining more than 97% of the activity after proteolytic treatment for 1 h. The superior characteristics of Man5A make it more advantageous for the application in the kraft pulp industry.

show abstract

Production, partial purification and properties of β‐mannanases obtained by solid substrate fermentation of spent soluble coffee wastes and copra paste using Aspergillus oryzae and Aspergillus niger

Cited by 37 publications

References 29 publications

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Xylanolytic enzymes production by Aspergillus niger GS1 from solid-state fermentation on corn stover and their effect on ruminal digestibility

Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola insolens Y1

Contact Info

Product

Resources

About