Stabilized Aerated Frozen Confection Containing Hydrophobin

41 Pages·2014·3.12 MB·English

US 20140050836A1
(19) United States
(12) Patent Application Publication (10) Pub. No.: US 2014/0050836 A1
COX et al. (43) Pub. Date: Feb. 20, 2014
(54) STABILIZED AERATED FROZEN (22) Filed: Aug. 14, 2012
CONFECTION CONTAINING
HYDROPHOBIN Publication Classi?cation
(75) Inventors: ANDREW RICHARD COX, (51) Int- Cl
SHARNBROOK (GB); NICHOLAS A236 9/20 (2006-01)
DAVID HEDGEs, SHARNBROOK A23G 9/38 (2006-01)
(GB); DAMIANO ROssETTI, (52) U-S- Cl
SHARNBROQK (GB); JAKOB USPC ........................................................ .. 426/565
BROBERG KRIsTENsEN, LANGA
(DK) (57) ABSTRACT
A frozen aerated confection is disclosed that is stable to
(73) Assigneer CONOPCO, INC-1 D/B/A UNILEVER, temperature abuse. A synergistic stabilization effect regard
EnglBWOOd Cliffs, NJ (US) ing the combination of hydrophobin, a Secondary protein and
a Co-surfactant is described that results in the observed sta
(21) Appl. No.: 13/585,257 biliZation.
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US 2014/0050836 A1 Feb. 20, 2014
STABILIZED AERATED FROZEN b. Adding hydrophobin and a Co-surfactant or Co-surfactants
CONFECTION CONTAINING to the chilled mix of step (a);
HYDROPHOBIN c. Aerating and freeZing the mix of step (b) to produce the
aerated and froZen product; and
BACKGROUND OF THE INVENTION d. Cooling the froZen product to a storage temperature of less
than about —15 C.
[0001] 1. Field of the Invention
[0002] The present invention relates to the production of an
BRIEF DESCRIPTION OF THE DRAWINGS
aerated froZen confectionery comprising of hydrophobin, a
Secondary protein, and a Co-surfactant (CSF). [0012] FIG. 1 is a graphical representation of Elastic modu
[0003] 2. Background ofthe Art lus for Example 1, samples A) HFBII, (B) HFBII+SMP and
[0004] It is desirable to make small siZe bubbles in aerated (C) HFBII+SMP+CSF (TWN20) at 5° C. as a function of
froZen confections that are stable to temperature abuse in time.
order to improve texture, palatability, and reduce caloric con [0013] FIG. 2 depicts SEM images for Example 1, HFBII
tent. It is Well understood that froZen confections such as (a, d), HFBII+SMP (b, e) and HFBII+SMP+CSF (TWN20)
sorbets, sherbets and ice cream experience temperature ?uc (c, f) for ice cream formulations described in Table 2. Images
tuations in the distribution chain and in consumers’ home shoW fresh samples (a to c) and after the storage test (d to f),
freeZers. This results in bubble growth and a degradation of Which includes the standard temperature abuse protocol.
the product quality and the palatability on consumption. It is [0014] FIG. 3 depicts SEM images of comparative samples
preferable to produce an ice cream With stable bubbles. containing 0.02 Wt. % TWeen 60 (a, d), 0.02 Wt. % Erythritol
[0005] US Patent publication no. 2006024417A, published (b, e), and 0.03 Wt. % Hygel (c, f). All samples include HFBII
on Feb. 2, 2006 to Berry et al. discloses aerated products (0.2 Wt. %) SMP (8.22 Wt. %)+comparative surfactant at
comprising hydrophobin Where the hydrophobin is used to concentration indicated. Images shoW fresh samples (a to c)
inhibit bubble coarsening. and after the storage test (d to f), Which includes the standard
[0006] US Patent publication no. 2008213453A published temperature abuse protocol. Samples correspond to equiva
on Sep. 4, 2008 to Burmester et al. discloses aerated food lent model formulations described in Table 3.
products and methods producing them, Where in the product [0015] FIG. 4 depicts SEM images of inventive samples
comprises hydrophobin and a surfactant. containing 0.02 Wt. TWeen 20 (a, d), 0.06 Wt. % TWeen 60 (b,
[0007] We have unexpectedly found that When the combi e), and 0.02 Wt. % PGE-O-80 (c, f). All samples include
nation of hydrophobin, at least one Secondary protein and at HFBII (0.2 Wt. %)+SMP (8.22 Wt. %)+inventive surfactant at
least one Co-surfactant (as those terms are de?ned beloW) are concentration indicated. Images shoW fresh samples (a to c)
used to make an aerated froZen confectionery product then: and after the storage test (d to f), Which includes the standard
[0008] The microstructure of the freshly produced prod temperature abuse protocol. Samples correspond to equiva
uct is preferable since the air bubbles siZes are generally lent model formulations described in Table 3.
smaller augmenting the bene?cial qualities described [0016] FIG. 5: is a graphical representation of Elastic
above. modulus for HFBI class II, HFBI class II+SMP and HFBI
[0009] The microstructure of the product after storage class II+SMP+CSF (TWN20) at 5° C. for indicated concen
and temperature abuse is preferable since the air bubbles trations as a function of time.
siZes are more stable and do not groW (coarsen) to the [0017] FIG. 6: is a graphical representation of Elastic
same extent as comparative cases. modulus for CU class II, CU class II+SMP and CU class
II+SMP+CSF (TWN20) at 5° C. for indicated concentrations
BRIEF DESCRIPTION OF THE INVENTION as a function of time.
[0018] FIG. 7 shoWs a schematic depiction of a micrograph
[0010] In one aspect of the invention is a froZen aerated
illustrating the guard frame concept for bubble siZe measure
food composition including but not limited to
ment.
a. at least 0.01 Wt. % of total hydrophobin(s) selected from the
group consisting of HFBII, HFBI or Cerato Ulmin or blends
DETAILED DESCRIPTION OF THE INVENTION
thereof added in isolated form to the food composition;
b, one or more Co-surfactants in the total concentration range [0019] In one aspect of the invention is a froZen aerated
of about 0.001 to less than about 0.3 Wt. % (preferably less food composition including but not limited to:
than about 0.1 or 0.2 Wt. %), and the Co-surfactant(s) to total a. at least 0.01 Wt. % of total hydrophobin(s) selected from the
hydrophobin Wt, ratio is in the range of about 0.02 to less than group consisting of HFBII, HFBI or Cerato Ulmin or blends
1.0. (Preferably the Co-surfactant to hydrophobin Wt. ratio is thereof added in isolated form to the food composition;
at least about 0.05, more preferably at least about 0.3 and b. one or more Co-surfactants in the total concentration range
preferably at most about 0.75); and of about 0.001 to less than about 0.3 Wt. % (preferably less
c. one or more Secondary protein(s) that are different from than about 0.1 or 0.2 Wt. %), and the Co-surfactant(s) to total
hydrophobin(s): Wherein said Secondary protein(s) are hydrophobin Wt. ratio is in the range of about 0.02 to less than
present in a total concentration range of about 0.25 to less than 1.0. (Preferably the Co-surfactant to hydrophobin Wt. ratio is
6.0 Wt. % (Preferably the total Secondary protein(s) are at at least about 0.05, more preferably at least about 0.3 and
least 0.5 or 1.0 Wt. % and at most 4 or 5 Wt. %). preferably at most about 0.75); and
[0011] In another aspect of the invention is a process of c. one or more Secondary protein(s) that are different from
making an aerated food composition including but not limited hydrophobin(s) Wherein said Secondary protein(s) are
to the steps of: present in a total concentration range of about 0.25 to less than
a. Blending the food composition ingredients together, mix 6.0 Wt. % (Preferably the total Secondary protein(s) are at
ing, and pasteurising; least 0.5 or 1.0 Wt. % and at most 4 or 5 Wt. %).
US 2014/0050836 A1 Feb. 20, 2014
[0020] Advantageously the total hydrophobin(s) concen The stability of the aeration can be assessed by monitoring the
tration is at most 1.5 Wt. %. Preferably the Co-surfactants is or volume of the aerated product over time and or the bubble size
are Water soluble non-ionic surfactant(s). More preferably the change over time.
Co-surfactant(s) are selected from Polysorbates, polyglyc
erol esters of alkyl or alkenyl fatty acids, diacetyl tartartic acid Microstructure
esters of mono-/di-glycerides, sucrose esters With an HLB
>about 8 orblends thereof. Most preferably the Co-surfactant [0028] The microstructure of frozen confections is critical
(s) has a minimum effective HLB value of about 8. Effective to their organoleptic properties. The air cells incorporated
HLB value is here de?ned as the arithmetic mean of the HLB into frozen confections are preferably small in size Which
values of a blend of Co-surfactants Advantageously the Co ensures that the frozen confections do not have a coarse
surfactant(s) is selected from TWeens 20, 60 or 80, PGE-O texture and also ensures that they deliver a smooth creamy
80; Panodan-Visco Lo 2000 and blends thereof. mouth-feel. In typical ice cream products, the air bubbles
coarsen over time (through distribution and storage) leading
[0021] Preferably the average bubble diameter (d3,2) is at
least 10% smaller after the standard temperature abuse pro to a degradation in quality.
tocol described beloW than the same product prepared the
Hydrophobins
same Way but absent either hydrophobin(s), Co-surfactant(s)
or if both are present then outside the total Co-surfactant(s) to
[0029] Hydrophobins are a Well-de?ned class of proteins
hydrophobin(s) ratio range of about 0.02 to less than 1.0.
(Wessels, 1997, Adv. Microb. Physio. 38: 1-45; Wosten,
Preferably the average bubble size is at least 20, 30, 40 or 50%
2001, Annu Rev. Microbiol. 55: 625-646) capable of self
smaller.
assembly at a hydrophobic/hydrophilic interface, and having
[0022] Preferably the average bubble diameter d(3,2) of the
a conserved sequence:
freshly prepared frozen product stored at beloW about — 1 5 ° C.
and pre-temperature abuse is at least 10% smaller, preferably
15% smaller, and more preferably 20% smaller than the same
product prepared the same Way but absent either hydrophobin
(s). Co-surfactant(s) or if both are present then outside the
total Co-surfactant(s) to hydrophobin(s) ratio range of about Where X represents any amino acid, and n and m indepen
0.02 to less than 1.0. dently represent an integer. Typically, a hydrophobin has a
[0023] In another aspect of the invention is a process of length of up to 125 amino acids. The cysteine residues (C) in
making an aerated food composition including but not limited the conserved sequence are part of disulphide bridges. In the
to the steps of: context of the present invention, the term hydrophobin has a
Wider meaning to include functionally equivalent proteins
a. Blending the food composition ingredients together mix
still displaying the characteristic of self-assembly at a hydro
ing, and pasteurising;
phobic-hydrophilic interface resulting in a protein ?lm, such
b. Adding hydrophobin and a Co-surfactant or Co-surfactants
as proteins comprising the sequence:
to the chilled mix of step (a);
c. Aerating and freezing the mix of step (b) to produce the
aerated and frozen product; and
d. Cooling the frozen product to a storage temperature of less
than about —15 C.
[0024] Preferably the process further includes the step of
extruding the frozen product from a freezer at a temperature or parts thereof still displaying the characteristic of self
of about —5 C or less. assembly at a hydrophobic-hydrophilic interface resulting in
[0025] All percentages, unless otherWise stated, refer to the a protein ?lm. In accordance With the de?nition of the present
percentage by Weight, With the exception of percentages cited invention, self-assembly can be detected by adsorbing the
in relation to the overrun. protein to Te?on and using Circular Dichroism to establish
the presence of a secondary structure (in general, ot-helix) (De
Frozen Confections Vocht et al., 1998, Biophys. 1.74:2059-68).
[0030] The formation of a ?lm can be established by incu
[0026] The term “frozen confection” means an edible con
bating a Te?on sheet in the protein solution folloWed by at
fection made by freezing a mix of ingredients Which includes
least three Washes With Water or buffer Masten et al., 1994,
Water. Frozen confections typically contain fat, non-fat milk
Embo. J. 13: 5848-54). The protein ?lm can be visualised by
solids and sugars, together With other minor ingredients such
any suitable method, such as labeling With a ?uorescent
as stabilisers, emulsi?ers, colours and ?avourings. Frozen
marker or by the use of ?uorescent antibodies, as is Well
confections include ice cream, Water ice, frozen yoghurt,
established in the art. In and n typically have values ranging
sherbets, sorbet and the like.
from 0 to 2000, but more usually m+n<100 or 200. The
de?nition of hydrophobin in the context of the present inven
Aeration
tion includes fusion proteins of a hydrophobin and another
[0027] The term aeration means that gas has been incorpo polypeptide as Well as conjugates of hydrophobin and other
rated into a product to form air cells. The gas can be any gas molecules such as polysaccharides.
but is preferably, particularly in the context of food products, [0031] Hydrophobins identi?ed to date are generally
a food-grade gas such as air, nitrogen or carbon dioxide or a classed as either class I or class II Both types have been
mixture of the aforementioned. The extent of the aeration can identi?ed in fungi as secreted proteins that self-assemble at
be measured in terms of the volume of the aerated product. hydrophobilic interfaces into amphipathic ?lms. Assem