Enzymatic Hydrolysis of Spent Coffee Ground

Jooste, Tracey; García-Aparicio, M. P.; Brienzo, Michel; Zyl, Willem H. van; Görgens, Johann F.

doi:10.1007/s12010-013-0134-1

Cited by 44 publications

(31 citation statements)

References 24 publications

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“…The broad signals result from the mixture of different hexose stereoisomers, which were derived from the various polysaccharides in the coffee matrix, e.g., galactomannan, cellulose, or mannan. 19,22 With this experiment, we could show that ochratoxin A is able to bind to the coffee matrix during roasting.…”

Section: ■ Results and Discussionmentioning

confidence: 84%

Matrix Binding of Ochratoxin A during Roasting

Bittner

Cramer

Humpf

2013

J. Agric. Food Chem.

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The mycotoxin ochratoxin A is degraded during coffee roasting by up to 90%. During this process, the two known degradation products, 14R-ochratoxin A and 14-decarboxy-ochratoxin A are formed. However, there is still an unexplained loss of more than 50% ochratoxin A. Here, we describe the binding of ochratoxin A to coffee polysaccharides via esterification as a further thermal reaction. This ester formation was studied by heating ochratoxin A with methyl α-d-glucopyranoside, a model compound to mimic polysaccharides. From this experiment, (22 → 6') ochratoxin A-methyl-α-d-glucopyranoside ester was isolated and characterized as a reaction product, showing the general ability of ochratoxin A for esterification with carbohydrates at roasting temperatures. Subsequently, a sample preparation protocol for the detection of ochratoxin A saccharide esters based on an enzymatic cleavage and purification using immunoaffinity chromatography was developed and applied. The detection was carried out by high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). Using this method, it was possible to detect ochratoxin A polysaccharide esters formed during roasting of artificially contaminated coffee, confirming the results of the previous model experiments. Thus, the formation of ochratoxin A esters is a further explanation for the loss of ochratoxin A during coffee roasting.

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Section: ■ Results and Discussionmentioning

confidence: 84%

Matrix Binding of Ochratoxin A during Roasting

Bittner

Cramer

Humpf

2013

J. Agric. Food Chem.

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“…Despite the large content of mostly carbohydrates that are of industrial interest, enzymatic hydrolysis of SCG treatment has not been widely studied . Kondamudi et al studied SCG for the production of biodiesel and fuel pellets because of its significant oil content, although its carbohydrate content was not considered.…”

Section: Introductionmentioning

confidence: 99%

Spent coffee ground mass solubilisation by steam explosion and enzymatic hydrolysis

Chiyanzy

Brienzo

García-Aparicio

et al. 2014

J of Chemical Tech & Biotech

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BACKGROUND: Instant coffee production generates large amounts of a waste known as spent coffee ground (SCG), which is rich in carbohydrate (∼50%), oil and aromatic compounds. RESULTS: Steam pretreatment by itself solubilised up to 10.7% of the SCG mass, which was recovered as soluble solids in the liquor from pretreatment. The highest extent of soluble solid recovery from pretreatment itself (10.7%) was obtained at 210 • C/15 min, while milder conditions (150-190 • C/10-12 min) recovered 2.6% soluble solids. Mannanase (recombinant strain of Yarrowia lipolytica) and cellulase (Acremonium, Bioshigen Co.Ltd, Japan) had an additive effect, with no indication of synergism observed. The best combinations of mannanase/cellulase cocktail for enzymatic hydrolysis were 0.5/0.82% and 0.01/0.91% (w/w), releasing 20.6% (g per 100 g raw SCG) and 22.6% (g per 100 g pretreated SCG) of soluble solids from untreated and pretreated SCG, respectively. By combining soluble solids recovered from steam pretreatment with the soluble products from subsequent enzymatic hydrolysis, a yield of 27.65% (g per 100 g SCG) was achieved. CONCLUSION: The pretreatment was effective in generating a material more amenable to enzyme action, thus requiring reduced enzyme dosages for subsequent hydrolysis compared with untreated SCG. The combined process showed significant technical feasibility for re-use SCG and may be considered to produce additional instant coffee product.

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“…nidulans, 14) and A. niger 29,30) and N. fischeri 15) have a high optimum temperature for activity at 80 °C. TtMan5A has the highest optimum temperature among the known fungal β-mannanases with Man5A1 and Man5A2 from T. leycettanus.…”

Section: )mentioning

confidence: 99%

Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase from <i>Talaromyces trachyspermus </i>B168 and Its Efficiency in Production of Mannooligosaccharides from Coffee Wastes

et al. 2018

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Highly thermostable β-mannanase, belonging to glycoside hydrolase family 5 subfamily 7, was purified from the culture supernatant of Talaromyces trachyspermus B168 and the cDNA of its transcript was cloned. The recombinant enzyme showed maximal activity at pH 4.5 and 85 °C. It retained more than 90 % of its activity below 60 °C. Obtaining the crystal structure of the enzyme helped us to understand the mechanism of its thermostability. An antiparallel β-sheet, salt-bridges, hydrophobic packing, proline residues in the loops, and loop shortening are considered to be related to the thermostability of the enzyme. The enzyme hydrolyzed mannans such as locust bean gum, carob galactomannan, guar gum, konjac glucomannan, and ivory nut mannan. It hydrolyzed 50.7 % of the total mannans from coffee waste, producing mannooligosaccharides. The enzyme has the highest optimum temperature among the known fungal β-mannanases and has potential for use in industrial applications.

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Enzymatic Hydrolysis of Spent Coffee Ground

Cited by 44 publications

References 24 publications

Matrix Binding of Ochratoxin A during Roasting

Matrix Binding of Ochratoxin A during Roasting

Spent coffee ground mass solubilisation by steam explosion and enzymatic hydrolysis

Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase from <i>Talaromyces trachyspermus </i>B168 and Its Efficiency in Production of Mannooligosaccharides from Coffee Wastes

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