Waste Biomass Valor (2014) 5:903917
DOI 10.1007/s12649-014-9311-x
REVIEW
Enzyme Production from Food Wastes Using a Biorefinery
Concept
Esra Uckun Kiran Antoine P. Trzcinski
Wun Jern Ng Yu Liu
Received: 13 February 2014 / Accepted: 30 June 2014 / Published online: 9 July 2014
Springer Science+Business Media Dordrecht 2014
Abstract According to Food and Agricultural Organiza-
tion (FAO), one-third of food produced globally for human
consumption (nearly 1.3 billion tonnes) is lost along the
food supply chain. In many countries food waste is cur-
rently landfilled or incinerated together with other com-
bustible municipal wastes for possible recovery of energy.
However, these two options are facing more and more
economic and environmental stresses. Due to its organic-
and nutrient-rich nature, theoretically food waste can be
converted to valuable products (e.g. bio-products such as
methane, hydrogen, ethanol, enzymes, organic acids,
chemicals and fuels) through various fermentation pro-
cesses. Such conversion of food waste is potentially more
profitable than its conversion to animal feed or transpor-
tation fuel. Food waste valorisation has therefore gained
interest, with value added bio-products such as methane,
hydrogen, ethanol, enzymes, organic acids, chemicals, and
fuels. Therefore, the aim of this review is to provide
information on the food waste situation with emphasis on
AsiaPacific countries and the state of the art food waste
processing technologies to produce enzymes.
Keywords Food waste
Biorefinery
Amylase

Protease
Lipase
Lignocellulosic enzymes
Pectinolytic
enzymes
E. Uckun Kiran
A. P. Trzcinski
W. J. Ng
Y. Liu
Advanced Environmental Biotechnology Centre, Nanyang
Environment & Water Research Institute, Nanyang
Technological University (NTU), Singapore 637141, Singapore
W. J. Ng
Y. Liu (&)
School of Civil and Environmental Engineering, Nanyang
Technological University, 50 Nanyang Avenue,
Singapore 639798, Singapore
e-mail: CYLiu@ntu.edu.sg
Introduction
Food waste (FW) is organic waste produced in food pro-
cessing plants, domestic and commercial kitchens, cafete-
rias, and restaurants. It accounts for a considerable
proportion of municipal solid waste all over the world [1].
According to FAO [2], nearly 1.3 billion tonnes of foods
including fresh vegetables, fruits, meat, bakery and dairy
products are lost along the food supply chain.
The amount of FW is continuing to increase due to the
increase in population and economical growth, particularly
in Asian countries. The annual amount of urban FW in
Asian countries would rise from 278 to 416 million tonnes
from 2005 to 2025 [3]. The highest absolute amount per
year was in China (82.8 Million tonnes (MT) followed by
Indonesia (30.9 MT), Japan (16.4 MT), Philippines (12
MT) and Vietnam (11.5 MT). However, the highest amount
of FW produced per capita was in New Zealand and
Australia with 280 kg/year, while it was around
120130 kg in Southeast Asia other than Cambodia
(173 kg/year). Although the absolute amount of food waste
in China is the highest, the waste production per capita is
the lowest (61 kg/year), while the waste production per
capita is 120 and 168 kg/year in Singapore and Hong
Kong, respectively [4, 5], showing that food wastage seems
more prevalent in high-income states. Food wastes have
been dumped, landfilled, incinerated, composted, digested
anaerobically and/or used as animal feed. In many Asian
countries FW is still dumped with other household waste in
landfills or dumpsites (Fig. 1). Unfortunately, the capacity
of the landfills is limited and would not be able to handle
increasing amount of FW [6].
In order to reduce its volume, FW is traditionally
incinerated with other combustible municipal solid wastes
for generation of heat or energy, particularly in Japan and
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904 Waste Biomass Valor (2014) 5:903917

Fig. 1 Waste treatment

methods in Asian countries [6
8]

Singapore. The incineration of FW is a favourable option
against landfilling in terms of overall energy recovery, and
emissions of greenhouse gases [9]. However, the inciner-
ation may not be an affordable approach for most low-
income countries due to the high capital and operating
costs [6]. It should also be noted that incineration of FW
can potentially cause air pollution [10].
Another approach to handle biodegradable FW is com-
posting which results in a valuable soil conditioner and
fertilizer [11]. Composting has a relatively low
environmental impact and a high economic efficiency
compared to other treatment methods. However, the high
moisture content of FW will lead to substantial release of
leachate [12]. Indeed, compost is more expensive than
commercial fertilizers and the current market of compost
produced from FW is limited [13].
Anaerobic digestion is another alternative which yields
methane and carbon dioxide as metabolic end products and
therefore could be feasible from an economic and envi-
ronmental point of view because methane is used as an

Table 1 Characteristics of mixed food waste

Origin pH Moisture Total solid VS/TS Total sugar Starch Cellulose Lipid Protein Ash References

Dining hall NR 79.5 20.5 95.0 NR NR NR NR 21.9 NR Han and Shin [16]
Cafeteria 5.1 84.1 15.9 15.2 NR NR NR NR NR NR Kim et al. [26]
Cafeteria 5.1 80.0 20.0 93.6 NR NR NR NR NR 1.3 Kwon and Lee [27]
MSW NR 85.0 15.0 88.5 NR NR 15.5 8.5 6.9 11.5 Rao and Singh [28]
Cafeteria 4.6-5 79.1 20.9 93.2 NR NR NR NR NR NR Ramos et al. [29]
Cafeteria NR 75.9 24.1 NR 42.3 29.3 NR NR 3.9 1.3 Ohkouchi and Inoue [30]
NR NR 87.6 12.4 89.3 NR NR NR NR NR NR Kim et al. [31]
Residents 4.9 80.8 19.2 92.7 NR 15.6 NR NR NR NR Pan et al. [22]
Dining hall NR 80.3 19.7 95.4 59.8 NR 1.6 15.7 21.8 1.9 Tang et al. [32]
Dining hall NR 82.8 17.2 89.1 62.7 46.1 2.3 18.1 15.6 NR Wang et al. [33]
Restaurant 3.9 80.0 20.0 95.0 70.0 NR NR 10.0 13.0 NR Zhang et al. [34]
Dining hall 5.6 82.8 17.2 85.0 62.7 46.1 2.3 18.1 15.6 NR Ma et al. [35]
Cafeteria NR 61.3 38.7 NR 69.0 NR NR 6.4 4.4 1.2 Uncu and Cekmecelioglu [36]
Food court NR 64.4 35.6 NR NR NR NR 8.8 4.5 1.8 Cekmecelioglu and Uncu [37]
Canteen NR 81.7 18.3 87.5 35.5 NR NR 24.1 14.4 NR He et al. [24]
Restaurant NR 81.5 18.5 94.1 55.0 24.0 16.9 14.0 16.9 5.9 Vavouraki et al. [23]
Restaurant NR 81.9 14.3 98.2 48.3 42.3 NR NR 17.8 NR Zhang and Jahng [38]

Total Solid, Total sugar, Starch, Cellulose, Lipid, Protein and Ash Contents were given in wt% on the basis of dry weight. Volatile solid contents were given as the
%VS ratio on total solid basis. NR: not reported

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Waste Biomass Valor (2014) 5:903917 905

energy source [9]. Hirai et al. [14] evaluated the environ-
mental impacts of FW treatment and found that utilising a
methane fermentation process prior to incineration reduces
approximately 70 kg CO2eq/tonne waste of the global
warming potential, due to the substitution effect. Food
waste is also used as animal feed. The disadvantages are its
variable composition and the high moisture content, which
favors microbial contamination [15]. To prevent this, ani-
mal feed is generally dried but greenhouse gas emission
increases depending on the energy usage during the drying
process, which is related to the water content of FW [10].
FW is mainly composed of carbohydrate polymers
(starch, cellulose and hemicelluloses), lignin, proteins,
lipids, organic acids (Table 1). Total sugar and protein
contents in FW are in the range of 35.569 and
3.921.9 %, respectively. Due to its inherent chemical
complexity, alternative treatment methods are currently
explored with emphasis on production of high value-added
products, such as biofuels, biodiesel, platform chemicals
and enzymes [1624]. In general, fuel applications (selling
price: $200400/ton biomass) and organic acids, biode-
gradable plastics & enzymes applications ($1000/ton bio-
mass) are usually creating more value compared to
generating electricity ($60150/ton biomass) and animal
feed ($70200/ton biomass) [25].
During the bioconversion of FW, its saccharification is
the rate limiting step. For an efficient biomass conversion,
carbohydrate components of FW should be hydrolyzed to
yield high concentrations of fermentable oligosaccharides
and monosaccharides. Hence, there is an increasing interest
in the production of biomass saccharifying enzymes,
mainly amylases and cellulases [39]. There are remarkable
amount of publications on the lab-scale production of
various industrial enzymes, such as proteases, amylases,
lignocellulosic enzymes and lipases using different types of
FW. Therefore, this review presents the state of the art of
production of various industrial enzymes from FW.
Enzyme Production
Various kinds of enzymes have been commonly used for
many industrial purposes. As such, enzyme production is of
important to sustain various industrial needs. So far, solid
state fermentation (SSF) has extensively explored for the
production of different enzymes with the ultimate aims to

Table 2 Amylase production from food wastes

Residual Microorganism Pretreatment Fermentation mode & Fermentation conditions Duration Achievements References
materials method vessel type (day)

Potato Bacillus subtilis Dried, SSF-250 mL flasks 40 C, pH 7, 65 % MC, 2 a-amylase [43]

peel ground, 10 % (v/w) inoculum (600 U/mL)
sieved
Potato Bacillus Dried, SSF-250 mL flasks 40 C, pH 7, 70 % MC, 2 a-amylase [43]
peel licheniformis ground, 10 % (v/w) inoculum (270 U/mL)
sieved
Coffee Neurospora Ground, SSF-250 mL flasks 28 C, pH 4.6, 60 % MC, 5 a-amylase [49]
waste crassa CFR steamed 1 mm PS, 107 spores/g ds (6,342 U/g
308 ds)
Potato Bacillus firmus Dried, SmF-250 mL flasks 35 C, pH 7.5, 1 % S 2 a-amylase [48]
peel CAS 7 ground, (676 U/mL)
sieved
Tomato Aspergillus Dried, SSF-plate-type SSF 28 C, pH 5 5 a-amylase [50]
pomace awamori milled, bioreactor (10.9 IU/g
sieved ds)
Bread Bacillus NR SmF- 1L flask with 30 C, pH 7 1 a-amylase [51]
waste caldolyticus 100 ml working vol (6.7 U/g ds)
DSM 405
Pea pulp Bacillus None SmF- flasks 70 C, 150 rpm 6 a-amylase [51]
caldolyticus (8.6 U/mL)
DSM 405
Food Aspergillus None SmF-250 mL flasks 30 C, pH 5, 120 rpm, 5 % 4 GA (137 [45]
waste niger UV-60 I/S U/mL)
Bread Aspergillus None SSF-petri plates 30 C, MC:1.8 (w/w, db), 6 GA (114 [52]
waste oryzae PS:20 mm, 106spore/gdS U/gdS)
S substrate, SSF solid state fermentation, SmF submerged fermentation, I/S Inoculum to substrate ratio, ds dry substrate, MC moisture content, PS
particle size, ds dry solid, GA glucoamylase

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Table 3 Lignocellulosic enzyme production from food wastes

123
Residual materials Microorganism Pretreatment Fermentation Fermentation conditions Duration Achievements References
method mode & (day)
vessel type

Banana wastes Bacillus Dried, ground, SSF-250 mL 35 C, pH 7, 400 lm PS, 70 % MC, 3 FPAse (2.8 IU/ds), CMCase (9.6 IU/g [65]
subtilis acid and alkali flasks 15 % (v/w) I/S ratio ds), Cellobiase (4.5 IU/g ds)
(CBTK106) pretreatment
Grape pomace Aspergillus Dried, milled, SSF- petri 30 C, 10 g S, 7 Xylanase (40.4 IU/g ds), Cellulase [69]
awamori sieved dishes 5 9 105 I/S, 60 % MC (9.6 IU/g ds)
Apple pomace Trichoderma Dried, crushed, SSF-250 mL 32 C, 70 % MC, 6 Cellulase (5.8 U/g ds) [66]
sp. sieved flasks 108 spores/flask
Banana peel Trichoderma Dried, crushed, SSF-250 mL 30 C, 65 % MC, 6 FPA(5.6U/g ds), CMCase (10.3 U/g ds), [67]
viride GIM sieved flasks 109 spores/flask b-glucosidase (3U/g ds)
3.0010
Tomato pomace Aspergillus Dried, milled, SSF-plate- 28 C, pH 5 5 Xylanase (195.9 IU/g ds), CMCase [50]
awamori sieved type SSF (19.7 IU/g ds)
bioreactor
Carrot, orange, Aspergillus Acid/base SSF-250 mL 30 C, pH 7, 1:1.5 to 1:1.75 S/M ratio 4 CMCase (310 U/gds), FPase (17 [62]
pineapple, potato niger NS-2 pretreatment flasks U/gds), b-glucosidase (33 U/gds)
peels, wheat bran using alkaline pretreated wheat bran
Apple pomace Aspergillus Drying, SSF-500 mL 30 C, 1.7-2 mm PS, 75 % MC, 7 FPase (113.7 IU/gds), CMCase [64]
niger crushing, flasks 7 (172.31 IU/gds), b-glucosidase
10 spores/g dS
NRRL-567 sieving (60.1 IU/gds), Xylanase (1412.6 IU/
gds)
Grape pomace and Aspergillus Dried, milled SSF-petri 30 C, pH 5, 70 % MC, 4.5 9 108 spores/g S. 15 Exo-PG (3.8 IU/gds), Xylanase [68]
orange peel awamori and sieved dishes (32.7 IU/gds), Cellulase (5.4 IU/gds)
Potato peel Aspergillus Dried, ground SSF 30 C, 107 spores/g dS, 50 % MC 3 FPase (0.015 U/mL), CMCase (0.023 [41]
niger U/mL), Xylanase(0.024 U/mL)
Mango Peel Trichoderma Alkaline SmF-250 mL 30 C, pH 7, 200 rpm 6 Cellulase (7.8 IU/mL) [63]
reesei pretreatment flasks
Passion fruit waste Pleurotus Dried, milled. SSF-250 mL 28 C in complete darkness 14 MnP (0.22 U/mL), b-xylosidase (4.76 [70]
pulmonarius flasks U/mL), b-Glucosidase (2.96 U/mL),
b-galactosidase (6.21 U/mL)
Passion fruit waste Macrocybe Dried, milled. SSF-250 mL 28 C in complete darkness 14 Laccase (10.2 U/mL), Pectinase (1.72 [70]
titans flasks U/mL), Endoxylanase (0.27 U/mL)
S substrate, SSF solid state fermentation, SmF submerged fermentation, I/S Inoculum to substrate ratio, DS dry substrate, S/M substrate to moisture ratio, MC moisture content, PS particle size,
ds dry solid, PG polygalacturonase, CMCase carboxymethylcellulase, MnP Manganese peroxidise, NR Not reported
Waste Biomass Valor (2014) 5:903917
 Table 4 Pectinolytic enzyme production from food wastes
Residual materials Microorganism Pretreatment Fermentation mode & Fermentation Duration Achievements References
method vessel type conditions (day)

Apple pomace Aspergillus None SSF- petri dishes 30 C, pH 4, 103 I/S 2 Pectinase (1,300 U/g S) [80]
foetidus
NRRL 341
Citrus waste Aspergillus None SSF- petri dishes 30 C 2 Pectinase (1,641 U/g S) [77]
foetidus
NRRL 341
Apple pomace Aspergillus None SSF- 15L horizontal 35 C 3 900 AJDA U/mL [79]
Waste Biomass Valor (2014) 5:903917

niger solid state stirred

tank reactor
Grape pomace Aspergillus Milled, SSF- petri dishes 30 C, 60 % MC 1 Exo-PG(40U/g S), Xylanase (40 U/g S) [74]
awamori sieved
Orange bagasse Botryosphaeria Dried, SSF-125 mL flask 28 C 6 Pectinase (32 U/mL), [78]
rhodina ground Laccase (46 U/mL)
MAMB-05
Orange waste Aspergillus NR SmF-Flask 30 C, pH 6, 3.5 Exo-PG (48.5 U/mL) [82]
giganteus 120 rpm, 1.107
CCT3232 spores/mL
Fruit residues (apple, lemon Aspergillus Dried, SmF-Flask 37 C, pH 3.5-5.5, 3 Endopectinase (6 U/mL), Pectinlyase (5 U/mL), [81]
peel, grape skin & tamarind flavipes FP- milled, 150 rpm, 1.106 Exopectinase (4.8 U/mL), Rhamno-
kernel) 500 sieved spores/mL galacturonase (33 U/mL)
Fruit residues (apple, lemon A. terreus FP- Dried, SmF-Flask 37 C, pH 3.5-5.5, 3 Endopectinase (3 U/mL), Pectinlyase (33 U/mL), [81]
peel, grape skin & tamarind 370 milled, 150 rpm, 1.106 Exopectinase (4.8 U/mL), Rhamno-
kernel) sieved spores/mL galacturonase (4 U/mL)
Tomato pomace Aspergillus Dried, SSF-plate-type SSF 28 C, pH 5 5 Exo-PG (36.2 IU/g ds) [50]
awamori milled, bioreactor
sieved
Lemon peel pomace Aspergillus Dried, SSF- column-tray 30 C, 70 % MC, 4 Pectinase (2.18 U/mL) [42]
niger Aa-20 ground bioreactor 194 mL/min AFR,
20.7 mm PS
Passion fruit waste Macrocybe Dried, SSF-250 mL flasks 28 C in complete 14 Pectinase (1.72 U/mL) [70]
titans milled. darkness
Orange peel Aspergillus Dried, Fixed bed bioreactor 25 C, 3.105 spores/ 7 Endo-PG (1.18 U/mL), [83]
niger ground mL Exo-PG (4.11 U/mL)
URM5162
S substrate, SSF solid state fermentation, SmF submerged fermentation, I/S Inoculum to substrate ratio, AFR air flow rate, DS dry substrate, MC moisture content, PS particle size, ds dry solid,
PG polygalacturonase, CMCase carboxymethylcellulase, NR not reported
907

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Table 5 Protease production from food wastes

Residual Microorganism Pretreatment method Fermentation Fermentation Duration Achievements References
materials mode & conditions (day)
vessel type

Date Bacillus sp. 2-5 Heat treatment & filtration SmF-125 mL 37 C, pH 10, 2 57,420 APU/ [91]
waste flask 125 rpm mL
Potato Saccharomyces NR SmF- 250 ml 28 C 5 360 U/mg [92]
waste cerevisiae flask
Fish meal Bacillus pumilus None SmF-20L 30 C, pH 7.5 2 7.05 U/mL [88]
MTCC 7514 bioreactor
Waste Aspergillus oryzae None SSF-petri 30 C, MC:1.8 (w/ 6 83.2 U/gdS [52]
bread plates w, db), PS:20 mm,
106 spore/gdS
Cuttlefish Vibrio Heat treatment, pressing, SmF- 250 mL 37 C, pH 8.7, 1 2,487 U/mL [94]
by- parahaemolyticus grinding, drying at 80 C flasks 200 rpm
products o/n, powdering
Shrimp Pseudomonas Heat pretreatment SmF- 250 mL 37 C, 200 rpm \1 15,000 U/mL [93]
waste aeruginosa MN7 (100 C, 20 min), flasks
drying, grinding
SmF submerged fermentation, SSF solid state fermentation, MC moisture content, PS particle size, S substrate, o/n overnight, NR not reported

Table 6 Lipase production from food wastes

Substrate Microorganism Pretreatment method Fermentation Fermentation Duration Achievements References
mode & vessel conditions (day)
type

Banana waste, melon Bacillus None SSF-Flasks 37 C, pH 7 1 148.9 U/g S [97]

waste, watermelon coagulans from melon
waste waste
Waste cooking oil Y.lipolytica None SmF- 5L 30 C, 6 0.93U/mL [105]
CECT 1240 stirred tank 400 rpm
bioreactor with
3L working
vol, fb
Waste cooking olive oil Aspergillus Filtration SmF-250 mL 28 C, pH 6, 3 645 U/mL [106]
and flasks 200 rpm
Penicillium
strains
Olive oil cake Y.lipolytica Alkaline SSF-150 mL 30 C, pH 7, 4 40 IU/g S [107]
NRLL pretreatment (3 % Erlenmeyer 55 % MC
Y-1095 NaOH) 20 C o/n flasks
Tri-substrate (wheat bran, A.niger None SSF-3*1 kg 30 C, 60 % 4 745.7 IU/gdS [108]
wheat rawa and coconut MTCC2594 tray type MC
oil cake) bioreactor
Seafood processing waste Bacillus Drying (80 C o/n) SSF-Flasks 50 C, pH 8, 3 2U/gdS [109]
altitudinis 80 % MC (Esterase)
Tuna by-products Rhizopus Heat pretreatment SmF- 1L flasks 30 C, pH 6, 3 23.5 IU/mL [110]
oryzae (100 C 20 min) 150 rpm
and filtration
Wheat bran with 2 % Aspergillus None SSF-Flasks 29 C, pH 7, 4 121.4 U/gdS [111]
olive oil flavus 65 % MC
Wheat bran with 2 % Aspergillus None SmF- 500 mL 30 C, pH 6, 8 1.46 U/mL [112]
olive oil niger J1 flasks 100 rpm
Wheat bran with 2 % Aspergillus None SSF- flasks 30 C, pH 6, 7 1.46 U/mL [112]
olive oil niger J1 65 % MC
S substrate, ds dry substrate, SSF solid state fermentation, SmF submerged fermentation, fb fed-batch, Y. lipolytica Yarrowia lipolytica, MC
moisture content, o/n overnight

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obtain high activity enzymes at lower cost, while using low
cost substrates as feed.
The So far, various kinds of FWs have been used to
produce different enzymes including proteases, cellulases,
amylases, lipases and pectinases particularly through solid
state fermentation (SSF) (Tables 2, 3, 4, 5, 6). SSF has
several advantages over submerged fermentation (SmF):
(i); cost and energy-effective; (ii) a simple fermentation
medium; (iii) superior productivity and (iv) less wastewater
generated [40]. Moreover, an easy control of bacterial
contamination and lower costs of downstream processing
make it more attractive. Dos Santos et al. [41] have eval-
uated SSFs efficiency for producing enzymes. It is appro-
priate for the production of enzymes, especially because of
the higher enzyme yields that can be obtained compared to
submerged fermentation [4244]. SSF provides a similar
environment to the microorganisms natural environment
which provides better conditions for its growth and
Fig. 2 Simplified process flow
diagram for FW based
biorefinery concept
909
enzymes production [44]. However, there are only a few
reports on SSF bioreactor design in the literature. The large
scale production of enzymes using SSF is challenging
because of difficulties in control of pH, temperature, aer-
ation, oxygen transfer and moisture content [40, 45].
Amylases
The amylase family has two major classes, namely a-
amylase (EC 3.2.1.1) and glucoamylase (GA) (EC 3.2.1.3).
a-amylase can hydrolyse starch into maltose, glucose and
maltotriose by cleaving the 1,4-a-D-glucosidic linkages
between adjacent glucose units in the linear amylose chain
[46], while glucoamylase hydrolyses the non-reducing ends
of amylose and amylopectin to glucose [47]. Amylases
have been widely used in the food, fermentation, textiles
and paper industries [46], and they are also employed for
the pre-treatment of agroindustrial and organic by-products
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910
to improve the bioproduct yield in subsequent processes.
High activity amylases can be produced from various kinds
of FWs, such as kitchen refuse [45], potato peel [43, 48],
coffee waste [49] and tomato pomace [50] via the opti-
mization of fermentation using different microbial strains.
However, it is difficult to compare the efficiency of various
processes as the produced enzymes activities are defined
in different ways (Table 2). The main advantage of enzyme
production from FW is that fermentation of FW would not
require harsh pre-treatments and extra nutrient
supplements.
Wang et al. [45] investigated the production of gluco-
amylase from FW by Aspergillus niger UV-60 using SmF,
and found that nutrient supplementation had no significant
influence on the glucoamylase production. Maximum glu-
coamylase activity of 137 U/mL was obtained using
3.75 % FW and 5 % (v/w, 106 spores/mL) inoculum at
30 C, 120 rpm for 96 h. A reducing sugar concentration
of 60.1 g/L could be produced from 10 % FW (w/v) within
125 min using the produced crude glucoamylase. Shukla
and Kar [43] also reported production of high activity a-
amylase from potato peels by SSF. Under optimal condi-
tions (40 C, pH 7, particle size of 1 mm with 6570 %
moisture content), alpha-amylase activities obtained using
B. licheniformis and B. subtilis were 270 and 600 U/mL,
respectively. In another study, a-amylase was produced
from potato peels by SmF with thermophilic isolate of
alkaline tolerant Bacillus firmus CAS7 strain [48]. Under
optimal conditions (at 35 C, pH 7.5 using 1 % of substrate
concentration), 676 U/mL of a-amylase was obtained. In
addition, Murthy et al. [49] used coffee wastes as sole
carbon source to produce a-amylase using SSF with a
fungal strain of Neurospora crassa CFR 308. a-amylase
activity of 4324 U/g dry substrate was obtained using 107
spores/g dry substrate, 60 % moisture content at 28 C, pH
4.6. It was also found that pre-treatment by steam improved
the accessibility of coffee waste and the a-amylase activity
of 6,342 U/g dry substrate was obtained.
FW can be used to produce high activity amylases using
suitable microbial strains. In studies of the lactic acid
production from FW, a saccharification step using com-
mercial amylases was included prior to the fermentation to
improve and ease the fermentation process [53, 54]. If the
enzyme production step can be integrated to the fermen-
tation system, the process costs could be lowered. The
consolidated biorefinery concept using enzyme production
process from FW is shown in Fig. 2. FW can either be used
to produce enzymes only (pathway B) or the enzymes
production is integrated into a bioprocess for producing
biofuels or chemicals through fermentation (pathway A).
Leung et al. [55] produced succinic acid (SA) from waste
bread through pathway A presented in Fig. 2. Aspergillus
awamori and Aspergillus oryzae produced an enzyme
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Waste Biomass Valor (2014) 5:903917
cocktail rich in amylolytic and proteolytic enzymes to
hydrolyze waste bread in SSF. The resulting fermented
solids were added directly to a bread suspension to gen-
erate a hydrolysate rich in glucose and free amino nitrogen.
The bread hydrolyzate was then used as the sole feedstock
for A. succinogenes fermentations, which led to the pro-
duction of 47.3 g/L SA with 1.16 g/g glucose, which is the
highest SA yield compared with other FW-derived media
reported to date. This consolidated process has potential to
transform FW into SA.
Lignocellulolytic Enzymes
Lignocellulolytic enzymes composed of cellulases, xylan-
ases and ligninases are mainly produced by several fungi.
They can degrade the lignocellulosic materials. For
example, cellulases have many applications in various
industries including food, animal feed, brewing and wine
making, agriculture, biomass refining, pulp and paper,
textile, and laundry [56]. The bioconversion of cellulose to
fermentable sugars requires the synergistic action of com-
plete cellulase system comprising of three enzyme classes:
endoglucanases (EC 3.2.1.4) which act randomly on solu-
ble and insoluble cellulose chains, exoglucanases (cello-
biohydrolases; EC 3.2.1.91) which liberate cellobiose from
the reducing and non-reducing ends of cellulose chains,
and b-glucosidases (EC 3.2.1.21) which liberate glucose
from cellobiose [57]. Xylanases have many applications in
food, feed, pulp and paper, brewing, wine making and
textile industries with or without concomitant use of cel-
lulases [58]. The hydrolysis of xylans mainly requires the
action of endo-b-1,4-xylanase and b-xylosidase. However,
the presence of other accessory enzymes is needed to
hydrolyse substituted xylans [59]. Lignin is an undesirable
polymer for biofuel production as it prevents the accessi-
bility of plant derived polysaccharides. However, lignin
derived materials can be used to develop valuable products
such as dispersants, detergents, drilling mud thinner, sur-
factants, coagulants and flocculants (for sewage and waste
water treatment), adhesives, graft polymers including
polyurethanes, polyesters, polyamines and epoxies and
rubbers [60, 61]. In order to degrade lignin polymers lig-
ninolytic enzyme mixtures consisting of laccases, lignin
peroxidases and Mn-peroxidase are utilized.
Lignocellulolytic enzymes are also used for the pre-
treatment of the agroindustrial and organic by-products to
improve the bioproduct yields in subsequent processes [62,
63]. Table 3 summarizes recent studies on lignocellulolytic
enzyme production using different FWs. Because the
enzyme activity can be defined in different ways, it is not an
easy task to compare the achievements and identify the best
method. However, fungal SSF is the most preferable method
generally [6267]. Krishna [65] reported that the total
Waste Biomass Valor (2014) 5:903917
cellulase production from banana waste was 12-fold higher
in SSF than that in SmF. However, Daz et al. [68] found that
SmF had higher xylanase production in comparison to SSF
because of better aeration in SmF. In fact, Umsza-Guez et al.
[50] showed a clear positive effect of aeration on xylanase
and carboxymethyl cellulase (CMCase) production using
SSF in a plate-type bioreactor.
In general, the optimum conditions for SSF depend not
only on the microorganism employed, but also on the type
of substrate. The incubation time, pH, temperature, particle
sizes and water content of the medium should be optimized
for given substrate and microorganism. Dhillon et al. [64]
investigated the effects of different inducers on cellulase
and hemicellulase production by Aspergillus niger NRRL-
567 using apple pomace as a substrate. The highest filter
paper cellulase (FPA) and b-glucosidase activities of
133.68 5.44 IU/gram dry substrate (gds) and
60.09 3.43 IU/gds, respectively were observed using
CuSO4 and veratryl alcohol. Similarly, the highest xylanase
activity of 1,412.58 27.9 IU/gds was obtained with ve-
ratryl alcohol after 72 h of fermentation, while the highest
CMCase activity of 172.31 14.21 IU/g ds was achieved
with lactose after 48 h of incubation. It has also been
reported that cellulase production using SSF was markedly
improved when lactose and corn-steep liquor was supple-
mented to apple pomace [66].
The cellulase production was found to be inhibited at
high concentration of reducing sugars when grape pomace
was used as substrate [68]. To mitigate such inhibition, the
nutrients composition of grape pomace was adjusted by
supplementing orange peel which induced cellulase pro-
duction. Moreover, Umsza-Guez et al. [50] also reported
that xylanase production from tomato wastes using SSF
was activated by Mg2?, but strongly inhibited by Hg2? and
Cu2?.
The substrate pre-treatments may affect the production
of cellulase and xylanase. For instance, Krishna [65]
investigated the effects of acid, alkaline and heat pre-
treatment on cellulase production from banana waste using
Bacillus subtilis. Although cellulase production was not
affected by alkali or acid treatment, it increased 6.84-fold
after pretreatment of FW by pressure-cooking at controlled
pH. This greatly improved substrate accessibility for
microbial growth, without the formation of monosaccha-
ride degradation products, such as furfural and hydroxy-
methyl furfural, which otherwise inhibit the cellulases [71].
Besides cellulases and xylanases, ligninases were also
produced from FWs by white rot fungi. Zilly et al. [70]
studied the oxidative and hydrolytic enzymes production
by SSF of yellow passion fruit waste using white-rot fungi
Pleurotus ostreatus, Pleurotus pulmonarius, Macrocybe
titans, Ganoderma lucidum, and Grifola frondosa. Under
the conditions used, the main enzymes produced were
911
laccases, pectinases, and aryl-b-D-glycosidases (b-glucosi-
dases, b-xylosidases, and b-galactosidases).
Biorefineries need to develop their indigenous enzyme
production processes along with their existing processes
(Fig. 2, pathway A), as commercial enzyme production
systems are still expensive to incorporate in biorefineries
[72]. As can be seen from the studies above, some strains
are producing different lignocellulosic enzymes from food
wastes simultaneously. These enzyme cocktails can be
used to hydrolyse biomass effectively at low cost for their
conversion to biofuels or platform chemicals. To further
improve the hydrolysis, different strains can be co-cultured
to produce enzyme solutions with synergistic hydrolytic
effects. Furthermore, some engineered strains can be used
to improve the saccharification yield.
Pectinolytic Enzymes
Pectinolytic enzymes, i.e. pectinases, degrade pectin
polymers in a sequential and synergistic way, by depo-
lymerisation and de-esterification reactions. Complete
degradation of pectin requires endo- and exo-acting po-
lygalacturonases and pectin- and pectate lyases as well as
enzymes rhamnogalacturonases that cleave the rhamno-
galacturonan chain [73]. Pectinases are widely used in
food industry particularly for juice and wine production as
well as many other industrial processes, such as textile,
plant fiber processing, tea, coffee, oil extraction, industrial
wastewater treatment [42, 74, 75]. The pectinases can be
produced via fungal SSF particularly by using Aspergillus
strains [73]. Industrially, pectinases can be produced from
pectin-containing wastes, such as citrus and orange wastes
[7678], apple pomace [79, 80], grape pomace [69] or
other fruit residues [81] without any harsh pre-treatment
owing to the nature of these substrates and the low
moisture content [74, 81]. Hours et al. [80] investigated
the pectinase production from apple pomace by SSF using
Aspergillus foetidus. After 36 h culture at 30 C with
nitrogen supplementation, an enzyme activity of 1,300
U/g was obtained (Table 4).
Pectinolytic enzyme was also produced from citrus
waste using Aspergillus foetidus in SSF [77]. It was found
that addition of yeast extract and minerals improved the
activity significantly after 36 h of culture. Berovic and
Ostroversnik [79] reported that the pectolytic enzyme
production from apple pomace was induced and/or
improved by cheap nutrients such as soya flour, wheat
bran, wheat corn and whey. They also mentioned that
moisture content was very important in enzyme production
and the highest activity was obtained at 38 % initial
moisture content. However, Ruiz et al. [42] reported that
70 % moisture content gave the highest pectinase activity
using lemon peel pomace.
123
912
Botella et al. [74] evaluated the feasibility of grape
pomace for the production of exo-polygalacturonase by
Aspergillus awamori in SSF. The particle size of the sub-
strate did not influence the enzyme production as it was
reported by Hours et al. [80], while the addition of carbon
sources and the initial moisture content of grape pomace
were found to have a marked influence on enzymes yields.
In another study, Giese et al. [78] carried out the produc-
tion of pectinases from orange waste by Botryosphaeria
rhodina MAMB-05 in SSF and SmF with and without
adding nutrients. A better microbial growth was observed
and the highest pectinase titre (32 U/mL) was obtained in
SSF of orange bagasse without adding nutrients.
Aeration is another important parameter affecting the
pectinase production. Umsza-Guez et al. [50] reported that
the forced aeration had a negative effect on exo-PG syn-
thesis, reducing its activity to half in a multi-layer packed
bed reactor. MacIel et al. [83] obtained the maximum endo-
and exo-PG activities of 1.18 U/mL and 4.11 U/mL,
respectively, using the reactor without aeration. Obviously,
a system without aeration is preferable because of opera-
tional and economic considerations.
The pH value of the medium can also affect the pec-
tinase production. Martnez Sabajanes et al. [81] investi-
gated the effect of different substrates (apple, lemon peel,
grape skin & tamarind kernel) and fungi (Aspergillus
flavipes FP-500 and Aspergillus terreus FP-370) on the
production of pectinases. The highest activities were
obtained using lemon peel. In both strains, acidic pH values
and high carbon source concentration favoured exopectin-
ase and endopectinase production, while higher pH values
and low carbon source concentration promoted pectin lyase
and rhamnogalacturonase production.
In summary, fruit wastes are preferable substrates for
producing high titers of pectinolytic enzymes using either
SSF or SmF. Process parameters including medium pH,
temperature, composition, inoculum size, moisture content
and particle size of the substrate and aeration highly
depend on the substrate and microbial strain. Statistical
experimental designs can be employed to optimize the
fermentation conditions by evaluating the effects and
interactions of the different parameters that rule a bio-
chemical system.
There is no industrial scale FW biorefinery facility
currently in operation. However, there are some studies
reporting the technical advances and engineering chal-
lenges of orange and lemon waste biorefineries [84, 85].
Direct utilization of citrus peel as animal feed is the sim-
plest option, requiring little infrastructure or investment,
while increasing the value of the waste material signifi-
cantly [85]. However, citrus peel contains high value
compounds such as pectin and D-limonene [86]. Pectin is
frequently used in food processing, while D-limonene is an
123
Waste Biomass Valor (2014) 5:903917
important essential oil for cosmetics, foods and pharma-
ceutical industries. D-limonene can be extracted using
suitable solvents. The residue after limonene extraction,
consisting mainly of pectin and lignocellulose, is an
excellent source for pectinolytic and lignocelluloytic
enzyme production and for the growth of microorganisms
to generate high value products such as industrial enzymes,
ethanol, methane and single cell proteins. Moreover, the
residual biomass i.e. lignin can be used as an energy
source.
Proteases
Proteases are one of the most important commercial
enzymes because of their wide range of applications in
food, pharmaceutical, detergent, dairy and leather indus-
tries [8790]. Some fungal strains such as Aspergillus,
Penicillium and Rhizopus and bacteria of genus Bacillus
have been reported as the most active producers of prote-
ases [51, 87, 91]. Although protease production from agro-
industrial wastes has been well studied in detail using both
SSF and SmF, the utilization of FWs for protease pro-
duction is not well documented (Table 5). Khosravi-Darani
et al. [91] used a newly isolated alkalophilic Bacillus sp. in
SmF of date wastes. High activity protease (57,420 APU/
mL) was obtained at pH 10, 37 C and the enzyme was
reported to be thermostable, indicating its possible utili-
zation in industrial applications. Afify et al. [92] investi-
gated the production of proteases from potato waste in a
submerged system using S. cerevisiae and studied the uti-
lization of remaining solid waste as a biofertilizer for plant
growth. The highest enzyme activity (360 U/mg) was
obtained using a fermentation medium containing 15 g
potato waste, at an initial pH of 6.0, at 20 C for 72 h. In a
study of Gupta et al. [88], fishmeal from sardine and pink
perch were evaluated as a sole carbon and nitrogen sources
using Bacillus pumilus MTCC 7514. The protease obtained
in medium containing only fish meal (4,914 U/mL) was
nearly two times higher than that using basal medium
(2,646 U/mL). The protease production was enhanced to
6,966 and 7,047 U/mL when scaled up from flask to 3.7
and 20 L fermenters, respectively. The crude protease was
found to have dehairing properties in leather processing. In
another study [93], P. aeruginosa MN7 was found to grow
and over-produce proteolytic enzymes (15,000 U/mL) in
media containing only shrimp wastes as sole substrate.
Although there are a few reports on protease production
from FW, the appreciable protease activities obtained on
different FW residues highlighted the potential of these
wastes.
Besides its potential utilization in many industrial
applications, proteases produced from FW can also be used
for biorefining different biomasses. Koutinas et al. [95]
Waste Biomass Valor (2014) 5:903917
evaluated an oat-based biorefinery for the production of
lactic acid as well as other value-added by-products, such
as b-glucan and antioxidant-rich oils using Rhizopus ory-
zae. Rhizopus oryzae produced a range of enzymes (glu-
coamylase, protease, phosphatase) during the hydrolysis of
complex macromolecules in oat. The utilization of waste
biomass and in situ produced enzyme cocktails in such a
biorefining strategy could lead to significant operating cost
reduction as compared to current industrial practices for
lactic acid production from pure glucose achieved by
bacterial fermentations.
Lipases
After proteases and carbohydrases, lipases (EC 3.1.1.3) are
considered as the third largest group based on total sales
volumes [96]. They are widely used for several applica-
tions in food, detergent, cosmetics, organic synthesis and
pharmaceutical industries. They are catalysing the hydro-
lysis of triacylglycerols to di- and mono- acylglycerols,
fatty acids and glycerol [9799]. They are also able to
catalyze alcoholysis, acidolysis, aminolysis, esterification
and transesterification under certain conditions [100].
Phospholipases are a sub-class of lipases that catalyse the
hydrolysis of one or more ester and phosphodiester bonds
of glycerophospholipids. They vary in site of action on
phospholipid which can be used for the modification/pro-
duction of new phospholipids for some applications in oil
refinery, health, food manufacturing, dairy and cosmetics
industries [101].
Most of the research has focused on high activity
extracellular lipase production using both SmF and SSF
via a wide variety of microorganisms including bacteria,
fungi, yeast and Actinomyces [98, 99, 102, 103]. Several
strains of commercial lipase producing fungi are quite
dominant, including Rhizopus, Rhizomucor, Aspergillus,
Geotrichum, Yarrowia and Penicillium species [104].
Recently, the production of lipase was investigated by
several researchers using different FW as substrates [97] or
by supplementing FW as inducer [105, 106]. Alkan et al.
[97] investigated the production of lipase from melon
waste by SSF using Bacillus coagulans. The highest lipase
production (78.1 U/g) was achieved after 24 h of cultiva-
tion with 1 % olive oil enrichment at 37 C and pH 7 by
supplementing sodium dodecyl sulphate (Table 6). The
best results were obtained by supplementing starch and
maltose (148.9 and 141.6 U/g, respectively), whereas a
rather low enzyme activity was found in cultures grown on
glucose and galactose (approximately 118.8 and 123.6 U/g,
respectively). Enzymes were inhibited by Mn2? and Ni2?
by 68 and 74 %, respectively. By contrast, Ca2? enhanced
enzyme production by 5 %. In a study of Dominguez et al.
913
[105] the biodegradation of waste cooking oil and its
application as an inducer in lipase production by Yarrowia
lipolytica CECT 1,240 were investigated. The addition of
waste cooking oil to the medium led to a significant
increase in extracellular lipase production by the yeast,
compared to oil-free cultures. Papanikolaou et al. [106]
explored the effects of different Aspergillus and Penicil-
lium strains using waste cooking oil as substrate. In car-
bon-limited medium, the highest amount of biomass (18 g/L)
with a lipid content of 64 % was obtained using Asper-
gillus sp. ATHUM 3482, while the highest extracellular
lipase activity (645 U/mL) was obtained by Aspergillus
niger NRRL 363. The studies above indicated the great
potential of FW either as substrates or inducers for lipase
production. Lipase production can be further improved
using mutant or engineered strains.
Lipases are also used for biodiesel production from
crude oil and fats [113] either in free or immobilized form.
Lipase production processes from FW can be integrated in
a biodiesel biorefining process to decrease the transesteri-
fication cost. Phospholipases are used for oil degumming
and for increasing fatty acid yields [114]. Further research
should be carried out on phospholipase production using
FW (Fig. 2, Pathway B).
Conclusions
The management of FWs has posed a serious economic and
environmental concern. This review highlighted the
potential of food waste to obtain high titres of industrial
enzymes such as amylases, cellulose, pectinases, proteases,
and lipases. The produced enzymes could be used in some
industrial applications depending on FW transportation
costs and purity requirements. Moreover, these enzymes
can be integrated in other bioprocesses in biorefineries to
produce biofuels and platform chemicals.
So far, biorefinery processes for the conversion of FW
into ethanol and other value-added products have only
been achieved at bench-top and pilot levels. There is no
industrial scale FW biorefinery facility currently in
operation. Therefore, it is not possible to conduct an
economical analysis for the proposed biorefinery systems.
However, considering the cost of defined medium prep-
aration in current commercial enzyme processes, the uti-
lization of low or no cost waste biomass could lead to
significant reductions in operating costs. However, diffi-
culties and costs associated with the collection/transpor-
tation of FW should also be taken into account.
Optimization and scale up studies need to be carried out
in order to exploit FW for enzymes applications at larger
scale.
123
914
Acknowledgments We would like to thank the National Environ-
ment Agency (NEA, Singapore) for financial support of this research
(Grant No: ETRP 1201 105).
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